Some Recent Books in Cell Biochemistry and Biology978-1-4615-7948...Some Recent Books in Cell...

Some Recent Books in Cell Biochemistry and Biology

As in previous volumes of SUBCELLULAR BIOCHEMISTRY, we are including a review section on various texts that may be of interest to our readers. The aim of these book notices is to be as informative as possible and to give the reader a full idea of the range and scope of the publication being reviewed. The books listed below will be discussed in this article.

1. Cell and Membrane Biology

Structure of Biological Membranes edited by Sixten Abrahamsson and Irmin Pascher, Plenum Press: New York and London, 1976,580 pp.

Cell Motility by Howard Stebbings and Jeremy S. Hyams, Longman: London and New York, 1979, 192 pp.

Methods in Membrane Biology, Vol. 8, edited by Edward D. Korn, Plenum Press: New York and London, 1977,368 pp.

Essentials of Cell Biology (2nd ed.) by Robert D. Dyson, Allyn & Bacon: Boston, Mass., 1978, 433 pp.

Cell Biology: A Molecular Approach (2nd ed.) by Robert D. Dyson, Allyn & Bacon: Boston, Mass., 1978, 616 pp.

2. Genetics and Viruses

The Biochemistry and Viruses by S. J. Martin, Cambridge University Press: Cambridge, 1978, 145 pp.

Extranuclear Genetics by Geoffrey Beale and Jonathan Knowles, Edward Arnold: London, 1978, 142 pp.

The Phylogeny of Human Chromosomes by Hector N. SeUllnez, Springer-Verlag: Berlin, 1979, 189 pp.

3. Muscle and CaH Transport

Smooth Muscle (British Medical Bulletin, Vol. 35, No.3) edited by Edith Btilbring and T. B. Bolton, The British Council: London, 1979, pp. 209-316.

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376 Some Recent Books in CeU Biochemistry and Biology

Calcium Transport and Cell Function (Annals of the New York Academy of Sciences, Vol. 307), edited by Antonio Scarpa and Ernesto Carafoli, New York Academy of Sciences: New York, 1978,655 pp.

4. General Biochemistry

Introduction to Biochemistry (2nd. ed.) by John W. Suttie, Holt, Rinehart and Winston: New York, 1977,434 pp.

Modern Concepts in Biochemistry (3rd ed.) by Robert C. Bohinski, Allyn & Bacon: Boston, Mass., 1979,600 pp.

Biochemistry: The Chemical Reactions of Living Cells by David E. Metzler, Academic Press: N ew York, 1977, 1129 pp.

1. CELL AND MEMBRANE BIOLOGY

The first book discussed in this section is Structure of Biological Membranes by S. Abrahamsson and I. Pascher. It is the proceedings of the 34th Nobel Symposium held in Sweden in 1976. Thirty contributions are included, ranging over a wide number of topics in membrane biology, biochemistry, and physical chemistry. Although it is now more than 4 years since the symposium was held, so high is the standard of the articles that the book's contents are still very relevant to contemporary work on biomembranes.

The book begins with an introductory chapter by S. Abrahamssoll, B. Dahlen, H. Lofgren, I. Pascher, and S. Sundell that shows how the various permitted packing arrangements of membrane lipids can give us an indication of the probable structure of biological membranes. The lipid layer of a surface membrane is visualized as consisting of the liquid region of the hydrocarbon matrix, the structural region of that matrix, the structural region of the polar part of the membrane and, finally, the surface functional region of the polar part. The behavior of the various regions is then related to the physicochemical properties of the lipids which make them up. Next, M. Anon, U. Pick, Y. Shahak, and Y. Siderer discuss proton transport through chloroplast membranes and its relation to energy conservation. The article strikingly demonstrates the close interrelationship between proton transport, light-induced electron transport, and A TP synthesis in chloroplasts, as well as reverse electronflow luminescence. Similar questions are discussed by M. Baltscheffsky in the next chapter on energy transduction in the chromatophore membrane. The organism Rhodospirillum rubrum was used as a model photosynthetic system; the absorbance of membrane-bound carotenoids changes during light-induced energy conversion, and the author discusses the significance of these alterations.

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The next article is a treatment of "Monomolecular Films and Membrane Structure," by D. A. Cadenhead, in which the author compares two contrasting physical states of monomolecular films (the "liquid condensed" and the "liquid crystalline" states) with the "gel" and "liquid crystalline" states of hydrated lipid bilayers. D. Chapman and B. A. Cornell then give a brief account of phase transitions, protein aggregation, and membrane fluidity. They discuss the various ways in which lipids can pack and give an interesting model showing naturally induced packing faults in a ball-bearing raft.

G. Dallner then discusses the biosynthesis and transport of microsomal membrane proteins. As the proteins move via the smooth endoplasmic reticulum to the Golgi system, the oligosaccharide element is continually being synthesized; final release into the cytoplasm is via a lipoprotein complex. There follows a short paper by L. L. M. van Deenen, J. de Gier, L. M. G. van Golde, I. L. D. Nauta, W. Renooy, A. J. Verkleij, and R. F. A. Zwaal on the asymmetry of lipids in the erythrocyte membrane and the fusion of plasma lipoproteins with the membrane. The relationships between phospholipid metabolism in plasma and erythrocyte are also discussed. A. Ehrenberg, Y. Shimoyama, and L. E. G. Eriksson then describe methods for evaluating EPR spectra of spin-labeled amphilic molecules in lipid bilayers. The method was applied to orientated and unorientated samples and used to study the influence of cholesterol on the physical state of dipalmitoyllecithin multibilayers.

L. Ernster, K. Asami, K. Juntti, J. Coleman, and K. Nordernbrand then describe the interaction of a protein that inhibits mitochondrial ATPase with submitochondrial particles. The authors suggest that the inhibitory protein may regulate energy transfer between the respiratory chain and the A TP generating system. E. H. Eylar then gives an account of the myelin membrane and of the basic proteins found in it. Their arrangement in the myelin membrane is discussed and their role in human demyelination diseases assessed. This is followed by an article entitled "Regulation of Pancreatic Phospholipase A2 by Different Lipid-Water Interfaces" by M. C. E. van Dam-Mieras, A. J. Siotboom, H. M. Verheij, R. Verger, and G. H. de Haas. This enzyme contains a specific "interface recognition site" that interacts with lipid-water interfaces. The site was studied in various modified phospholipases in which the N-terminal alanine had been substituted by other amino acids or by amino acid chains.

C. R. Hackenbrock then presents a comprehensive account of the molecular organization and fluidity of the mitochondrial membrane. In view of the importance of the subject, it may be of interest to quote in full Hackenbrock's assessment of current views on mitochondrial organization:

The picture that emerges is that of a highly effective concentration of integral proteins partitioned in a polar bilayer phospholipid environment of relatively low viscosity and high fluidity. The polar environment provides for a precise vertical

378 Some Recent Books in Cell Biochemistry and Biology

orientation of the integral metabolically active membrane proteins. The fluid environment provides for lateral translational and rotational mobility of the integral metabolically active membrane proteins which can diffuse laterally, depending on their specific metabolic role, either independent of or in association with other integral proteins.

J. N. Hawthorne then gives an account of the role of triphosphoinositide in myelin and plasma membranes in Ca2+ ion binding. The author also discusses the role of phosphatidyl inositol and phosphatidic acid in the release of neurotransmitters. K.-A. Karlsson then gives an account of sphingolipids in cell-surface membranes. He surveys the ceramide composition of a number of cells, postulates that sulfa tides and acid phospholipids are involved in the action of the Na + -K+ pump, and assesses the role of sphingolipids as surface antigens. J. A. Lucy then describes the use of the hen erythrocyte membrane as a model system for studies on membrane fusion. He suggests that "fusogenic lipids" alter the polar regions of membrane phospholipids and that as a result the membranes become more permeable to Ca2+ ions. This sets off a series of changes that ultimately favor membrane fusion. I. Lundstrom then discusses the structure and electrical properties of lipid-water systems. The lateral conductivity, Raman spectra, and light-scattering properties of an artificiallamellar lipid-water system were examined and the artificial system compared to biomembranes. A. Tardieu, C. Sardet, and V. Luzzati then present the results of X-ray scattering studies of bovine rhodopsin. Using a detergent-rhodopsin complex, they concluded that thin elongated rhodopsin molecules (more than 80 A long) span the flat detergent micelle.

P. BrUlet, G. M. K. Humphries, and H. M. McConnell then discuss the immunochemistry of model membranes containing spin-labeled haptens. They include studies on spin-label hapten resonance spectra and on complement fixation. Next, M. D. Hous)ay, A. Johannson, G. A. Smith, T. R. Hesketh, G. B. Warren, and J. C. Metcalfe present an article on the coupling of the glucagon receptor to adenylate cyclase. They describe various models that have been proposed to explain the relationship between hormone receptors and adenylate cyclase. This is followed by an account of peptide ionophores by Yu. A. Ovchinnikov. In particular, he discusses valinomycin, enniatin B, gramicidin, and their analogues. The article includes detailed biochemical and physicochemical studies of various ionophores and of their interaction with liposomes.

G. D. Eytan, G. Schatz, and E. Racker then describe experiments on the incorporation of integral membrane proteins into liposomes. They give details of the sequential insertion of various mitochondrial multienzyme complexes and compare the results of these in vitro systems with what is known of mitochondrial membrane assembly in vivo. P. R. Cullis, B. de Kruijff, A. E. McGrath, C. G. Morgan, and G. K. Radda then discuss lipid asymmetry and molecular motion in biomembranes with particular reference to the behavior

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of chromaffin granules. They describe various model systems and also give details of the interesting technique in which the decay times of positrons introduced into the lipid matrix are measured. O. Renkonen, M. Pesonen, and K. Mattila then give an account of the oligosaccharides of the membrane glycoproteins of the Semliki Forest virus. They propose a complex structure involving a branched arrangement of N-acetyl neuraminic acid, mannose, and Nacetyl glucosamine groups attached to a peptide framework.

A. M. Scanu then discusses the use of phospholipases as probes for circulating lipoproteins. In particular, the effects of lipolytic enzymes of low-density lipoprotein LDL2 and high-density lipoprotein HDL} are described. Next, S. J. Singer gives an account of the fluid mosaic model of membrane structure. He considers various thermodynamic aspects of membrane fluidity and also discusses the molecular asymmetry of membranes and the mechanism of transport of hydrophilic ligands through membranes. J. C. Skou discusses the coupling of the passive flux of N a + and K + ions to the active transport of these ions and analyzes the role of the "i-site" (inside) and the "o-site" (outside) in Na+ and K+ transport. The relative merits of one-site and two-site models are discussed. W. Stoeckenius, S-B. Hwang, and J. Korenbrot then give an account of proton translocation by bacteriorhodopsin in lipid vesicles. In intact cells it is difficult to examine the relationships between light absorption, proton gradients, and membrane potential. Use of a reconstituted model system overcomes these difficulties and the article assesses the results of studies of these parameters in the model system.

C. Tanford then discusses the state of association of membrane proteins. By using appropriate detergents, membrane proteins may be isolated as a part of a detergent micelle in a form similar to that in the membrane, and then subjected to classic physicochemical techniques. This approach is used to study the subunit structure and organization of cytochrome bs and sarcoplasmic reticulum Ca2+ ATPase. The next chapter on membrane electrostatics is by the late H. Traiible and deals comprehensively with surface electrostatics, the effect of electrostatic forces on membrane structure, ion pulses in membranes, electrostatic regulation of membrane phase separations, and electrostatic coupling between two layers of a membrane. The book ends with a chapter by G. Vanderkooi and J. T. Bendler entitled "Dynamics and Thermodynamics of Lipid-Protein Interactions in Membranes." The free energy of mixing of lipids and membrane proteins is discussed, as well as the athermal entropy of mixing. Hamaker constants are given for lipid-lipid, protein-lipid, protein-protein interactions, and the use of the generalized Guggenheim method is discussed. The book includes a short subject index.

As the above detailed survey shows, Structure of Biological Membranes covers a broad canvas and contains detailed and authoritative chapters by established experts. However, as the reader may well have noticed in the above survey, there has been no clear attempt to group related chapters, so that one


has to leap rather suddenly from one area of membrane biology to another. In fact, many of the chapters are quite closely related, and had the editors departed from the rigid method of listing the articles in simple alphabetic order, a more stimulating and readable book would have been presented. Nevertheless the publication is a most useful addition to the now regrettably overwhelming literature on biological membranes.

The next book to be discussed is Cell Motility by H. Stebbings and J. S. Hyams and contrasts strongly with the rather massive multiauthor text just reviewed, being written by only two authors and only running to 192 rather small pages. This interesting and well-presented book is part of an excellent Longman series edited by I. D. J. Phillips entitled Integrated Themes in Biology, which includes such useful monographs as Mitochondria by P. A. Whittaker and S. M. Danks.

In the preface the authors stress the great current interest in cell motility in all its aspects as a result of the appreciation of the widespread occurrence of microtubules and microfilaments. The book begins with an account of the structure and function of striated muscle, as the most highly specialized system capable of converting chemical energy in the form of ATP into useful mechanical work. The structural organization of striated muscle is described, and the biochemistry of muscle proteins surveyed. The now famous sliding filament theory is briefly but elegantly presented, and there is a short account of the control of contractility. The next chapter deals with microtubules and microfilaments. The morphology of microtubules is discussed in detail and there is a full account of microtubule biochemistry including the heterodimer model, the mode of action of colchicine, the Vinca alkaloids, and other spindle poisons, as well as what we know of microtubule assembly both in vivo and in vitro. The identification and morphology of microfilaments is then described and the role of actin discussed. Evidence for the existence of cytoplasmic myosin is assessed and the general role of contractile proteins discussed. There is an account of actin-membrane associations, and the chapter ends with a critical analysis of the efficacy of cytochalasin B as a specific disrupting agent for microfilaments.

The next chapter deals with cilia, flagella, and axostyles. After an account of ciliary and flagellar movement, there is a full treatment of the structure and biochemistry of the axoneme and of the reactivation of cilia and flagella. The chapter ends with a description of the fascinating axostyle found in some anaerobic flagellates; this is a ribbonlike bundle of an ordered arrangement of singlet microtubules and is an ideal model system for the study of ciliary and flagellar movement. (In passing, it may be mentioned that these elegant and informative observations on the axoneme provide a good example of the impossibility of predicting the scientific usefulness of a given field of study in advance. The organism mentioned is the anaerobic flagellate Saccinobacculus, which inhabits the hindgut of the wood-eating roach Cryptocercus. This appar-

Some Recent Books in Cell Biochemistry and Biology 381

ently obscure organism may, however, provide information of central importance to cell biology.)

The authors then deal with cell movements and contractile proteins. They describe the acrosome reaction in invertebrate sperm, shuttle streaming in slime moulds, amoeboid movements, and brush-border contraction. The next chapter deals specifically with movements within cells. The role of microtubuies in intracellular transport is extensively and critically discussed, and there is an account of protoplasmic streaming and the possible role of microfilaments in this process. The next chapter deals with mitosis and cytokinesis. The structure of the mitotic spindle is described, as well as the distribution of spindle microtubules. The evidence for the presence of actin in the spindle is assessed and there is a useful account of the "sliding microtubule model" as a mechanism of mitosis. The chapter ends with a brief account of cytokinesis and of the contractile ring. The book ends with a short description of contractile movements in ciliates such as Stentor and Vorticella and of various "pendulous" and "gliding" movements of such sporozoans as Selenidium and Gregarina.

There is a short subject index and each chapter is amplv furnished with detailed references and a basic list of suitable review articles and monographs. The text is admirably illustrated throughout with high quality diagrams and electron micrographs. Cell Motility clearly shows that we have now entered a phase of dramatic unification in our understanding of the mechanics of a wide range of biological processes. The terms filament, tubule, actin, and myosin occur again and again throughout the text, leaving one with the overwhelming impression that just as a relatively few amino acids can produce an infinite variety of proteins, so can a few contractile and fibrous elements produce a wealth of contractile and motile activities. Stebbings and Hyams's book is an excellent and stimulating introduction to this exciting new synthetic phase of cell biology.

The next book to be discussed is Essentials of Cell Biology by Robert D. Dyson. This is an undergraduate textbook, and the author states in his preface: "The objective of this book is to present a unified description of cellular structure and function at the introductory level." The first chapter surveys the cell theory, the main structural features of prokaryotic and eukaryotic cells, and techniques for investigating cell structure. Some excellent electron micrographs show the main features of the major cellular elements and illustrate the section on methods. The next chapter is entitled "Membranes and Macromolecules" and in a most original way deals with the chemistry of lipids, proteins, and carbohydrates at the same time as the main features of membranes and macromolecular assembly are discussed. The student is therefore encouraged to view the study of the chemistry of macromolecules as being intimately connected to an understanding of the way in which these macromolecules come together to form organized cell structures.

The next chapter discusses bioenergetics and cellular homeostasis. An


account of basic thermodynamics leads on to an explanation of enzyme action, metabolic feedback, and ATP-coupled reactions. Glycolysis is treated as an example of an integrated metabolic pathway and there is a brief account of biological oxidation. Thus thermodynamics, enzymology, and metabolic pathways are not presented as separate topics, as is so often the case, but are examined in an interlinked and intellectually satisfying manner. Genes and their regulation are the next major topic, and here we have accounts of general genetic concepts, the chemical nature of the gene, DNA structure, the nuclear envelope, chromosomes, the genetic code, and transcription. Again, the various subsections interlock naturally. From transcription the author proceeds to an account of protein biosynthesis, and via a description of the endoplasmic reticulum and Golgi apparatus, to a survey of the main aspects of secretion.

The plasma membrane is then discussed in a chapter that includes accounts of cellular recognition, membrane transport, active transport, endocytosis, lysosomes, membrane turnover, and biosynthesis. Mitochondria, chloroplasts, and peroxisomes are discussed in one chapter that includes accounts of the Krebs' cycle, electron transport, oxidative phosphorylation, photosynthesis (light and dark varieties), peroxisomal metabolism, and organelle evolution.

Excitability, contractility, and motility are discussed next in a chapter that includes accounts of muscle contraction, nerve, and muscle excitability, excitation-contraction coupling, cilia, and flagella. Next follows a chapter on DNA replication, mitosis, meiosis, and cytokinesis. The final chapter gives an account of cellular differentiation. There is an excellent glossary of terms at the end of the book, followed by a medium-size subject index. Each chapter contains rich illustrations with excellent structural diagrams and well-chosen electron micrographs and ends with a well-set-out reference list subdivided according to subject. All in all, reading Essentials of Cell Biology is a most pleasurable experience. Its most admirable feature is the way in which the "classic" sections on glycolysis, the Krebs' cycle, enzymology, and protein structure are neatly woven into the descriptions of organelle structure and function. Let us hope that students who have based their studies on this book will come away with as integrated a view of the cell and its biochemical constituents as its author has.

Dyson's other book (Cell Biology: A Molecular Approach) was reviewed in detail in Sub-Cellular Biochemistry, Volume 3 (pp. 371-372), and the review ended with the statement that it is " ... a most excellent contribution to the educational literature in the field and can be recommended without hesitation to all cell biologists." We have now received the second edition for review, and it is similar to the first, only better. The author has taken into account many readers' suggestions and has more on membrane structure and function, new material on contractility and motility, plus some new clinically


relevant material. There is no doubt that Essentials of Cell Biology and Cell Biology: A Molecular Approach represent two major landmarks in the evolution of student texts in cell biology.

The final book to be considered in this section on cell and membrane biology is Volume 8 of Methods in Membrane Biology edited by E. D. Korn. The first article is by P. Zahler and V. Niggli and surveys the use of organic solvents in membrane research. The authors discuss the difficulties of working with amphipathic proteins, as a medium suitable for the polar regions is unsuitable for the nonpolar parts of the molecule, and vice versa. The "ideal" liquid medium for the fractionation of membrane proteins would tolerate both the charged and hydrophobic regions without causing extensive secondary unfolding of the molecule. In many ways detergents answer this need-unfortunately their use results in the isolation of detergent-membrane protein complexes, and it is often difficult to distinguish which properties are attributable to the protein and which to the detergent. Zahler and Naggli survey the wide variety of organic solvents that have been used to overcome these difficulties and give useful details of their physical properties. They also describe the application of the most commonly used solvents to membranology. They include a useful appendix that describes extraction methods for total lipids, serum phosphatides, and membrane proteins. The chapter thus usefully brings together data on a technique that is gaining increasing importance in the investigation of hydrophobic interactions in membranes.

The next article is by R. A. Klein and P. Kemp and surveys in a most comprehensive way recent methods fdr the elucidation of lipid structure. As our understanding of the molecular organization of membranes improves, it becomes more important to have a precise knowledge of the chemical structure of membrane lipids. This article shows how powerful contemporary analytical techniques have been applied to the investigation of lipid structure. The authors survey separation techniques, methods for lipid identification, the analysis of stereoisomers, mass spectrometry, and proton and carbon-I 3 nuclear magnetic resonance spectroscopy. There is also a useful section on artifacts and contaminants. The next chapter by M. Kates is entitled "Synthesis of Stereoisomeric Phospholipids for Use in Membrane Studies." Chemical studies on lipids clearly depend on the supply of uncontaminated lipids of known composition and stereochemical configuration. Regrettably, lipids isolated from natural sources often do not meet these requirements, so that the use of lipids chemically synthesized by unambiguous routes is important in lipid (and hence membrane) research. Procedures for the synthesis of a wide range of phospholipids are given, and there is also information on the synthesis of alkyl and alk-I-enyl ether analogues of phospholipids (e.g., various plasmalogens). One is struck on reading Kates's article by the great variety of natural phospholipids and the superficiality of the view that only phosphatidyl choline, serine, and ethanol-


amine are of interest. The article should help considerably to improve the precision of studies on the chemical constitution of membrane phospholipids.

The last chapter of this useful volume is by B. J. Gaffney and S-c. Cben and deals with spin-label studies of membranes. The authors begin with a historical treatment of the application of electron paramagnetic resonsance spectroscopy to the study of biomembranes; the various nitroxides used are described and data are presented of diffusion constants of lipids in membranes. There is a useful theoretical section on the analysis of paramagnetic spectra and of the effects of molecular motion on these spectra. The application of these techniques to the study of lipids and proteins in membranes is then surveyed and the results compared to those obtained by other physical techniques such as freeze-fracture electron microscopy and X-ray diffraction.

Volume 8 of Methods in Membrane Biology thus continues the tradition of this series of providing detailed, useful, and expert surveys of methodology in membrane research.

2. GENETICS AND VIRUSES

The first book to be considered in this section is The Biochemistry of Viruses by S. J. Martin. This is a short introductory textbook" ... designed to provide a rapid overall picture of virology at the molecular level," and it succeeds admirably in its task. It is written in essay style, and the various diagrams, structural formulas, and plates are well chosen and clear. After a brief history of virology, the author discusses the classification of viruses. Methods of quantitatively assaying viruses are then described and an account is given of various methods of purification of viruses. The architecture of viruses is then discussed and the author explains how the fact that they appear to be formed by self-assembly greatly limits the range of morphologies encountered in viruses. Essentially two main repeating patterns are used-helical symmetry, which gives rise to rod-shaped viruses, and icosahedral symmetry, which gives rise to spherical or spheroidal viruses. The author surveys the molecular organization of turnip yellow mosaic viruses, picornaviruses, including adenovirus, complex viruses, such as paramyxoviruses, and finally the bacteriophages.

The next chapter deals with the "Strategy of Virus Infection" and describes the physical processes involved (e.g., the attachment of the virus to the host, the penetration of infective material, and the "uncoating" of the virus); the main biochemical features of viral infection are also given. The process of infection is described by the author in an excellent turn of phrase as a "biochemical coup d'etat," and the chapter shows in full detail the elegant devices whereby the imposter takes over the informational and replicative


machinery of the host and subverts it for the manufacture of viral particles. The author, with another graphic expression, calls viruses "Invaders of the Genosphere" and draws analogies between their catastrophic effects and those of man, who he describes as "Invader of the Biosphere." The last chapter discusses the evolution of viruses, the development of vaccines and research into antiviral chemotherapeutic agents. The possible benefits, but also the potential hazards, of genetic engineering involving viruses are discussed .

. All in all, The Biochemistry of Viruses is pleasant and informative reading with a stimulating seasoning of humor and philosophy. It is a most useful introduction to the world of viruses and successfully captures the author's sense of enthusiasm and wonder at these sophisticated biological hijackers.

The next book in this section is Extranuclear Genetics by G. Beale and J. Knowles. This excellent monograph is aimed at a wide audience, merely assuming that the readers have an elementary knowledge of molecular biology and basic genetics. The preface contains the all-too-common "exclusion clause" viz.:

Organelle genetics, and even more the genetics of bacterial plasm ids, are such rapidly advancing areas of research that we cannot hope our account is completely up-to-date even at the time of writing . ... [italics added]

Thus even as we write we are out of date. Worse, we become out of date as we read! If we have to journey through hundreds of pages of multiauthor, jargonreplete, pseudolegalistic prose that makes up so much of the contemporary "literature" our out-of-datedness increases with our sense of confusion and frustration. How refreshing, therefore, to read a book that has a mere 120 or so pages, with sufficient but not excessive tables and figures, and-glory of glories-is written in comprehensible English, not moleculobiological newspeak.

The introduction sketches the main features of non-Mendelian or extranuclear inheritance and reminds us forcibly how until recently genetics had been dominated by the" ... extremely rigid, mechanistic concepts of classical geneticists .... " Thus the authors quote Morgan as having written in 1926: "The cytoplasm may be ignored genetically." It is not generally realized, with respect to this remark by Morgan, that there was considerable evidence for non-Mendelian "aberrant" genetic systems early in 20th century, and it is quite false to regard the development of the science of cytoplasmic inheritance as having occurred after the discoveries of mitochondrial and chloroplastal DNA.

The authors then deal with the mitochondrion, briefly surveying the structure and properties of mitochondria and then giving details of the mitochondrial biosynthetic apparatus. There is an account of the mechanism of repli-


cation of mitochondrial DNA and of the principal phenotypic effects of changes to mitochondrial genes (petiteness in yeast, poky variants in Neurospora, and more recently various drug-resistant phenomena in a variety of cell types). There is a full section on recombination of mitochondrial genes and also of the recent advances in the mapping of the mitochondrial genome. The particular complexities that arise from two genetic systems in mitochondrial biogenesis are then discussed, and the chapter ends with a short account of the kinetoplast and kinetoplast DNA in trypanosomes and similar organisms. The next chapter on the chloroplast follows the same general design as the chapter on mitochondria. The main features of the findings with the two organelles are strikingly similar-each has its own limited biosynthetic apparatus, each relies on the interaction of two genetic systems, and the major gene products in both organelles are ribosomal RNAs and hydrophobic membrane-bound proteins. There are differences in detail, however (e.g., the chloroplast can synthesize a soluble protein, fraction I protein large subunit, and appears to have greater coding capacity than the mitochondrion); nevertheless the similarities between the two systems are very thought-provoking.

There follows a chapter on bacterial plasmids. In view of the absence of a defined bacterial nucleus enveloped in a limiting envelope or membrane, it is not immediately obvious that plasmids should be considered in a book entitled Extranuclear Genetics. However, the authors justify this on the grounds that one can regard the main mass of bacterial DNA as constituting a chromosome (albeit not partitioned in its own enevelope), and the plasm ids can be looked on as "accessory" genetic elements. The authors stress that the plasmid is an excellent model for the study of extrachromosomal phenomena. After a brief description of F, R, and Col plasmids, there are full accounts of the replication of plasmid DNA, plasmid transfer, recombination, and mapping. There is also a useful section on artificial plasmids and on genetic engineering using plasmid vectors.

The next chapter is entitled "Endosymbionts and Viruses as Agents of Extranuclear Heredity" and contains some fascinating examples of external agents that can influence extranuclear inheritance. The examples given include, inter alia, the kappa particles of Paramecium aurelia; a rickettsial ike microorganism apparently responsible for incompatibility between certain mosquito strains; various spiroplasmalike symbionts and their associated viruses that appear to be involved in the production of abnormal sex ratios in the offspring of certain species of Drosophila; the "sigma" virus, which confers CO2 sensitivity on some strains of Drosophila melanogaster; and finally RNAcontaining viruslike particles in "killer" strains of Saccharomyces cerevisiae and the fungus Ustilago maydis. The authors stress that these agents, originally thought to be examples of an unusual biological phenomenon, probably represent a widespread process whereby extraneous elements interfere with the


genetic system of a host. Thus kappa was at first thought to be a special case in P. aurelia. It now transpires that almost every species of ciliate as well as many other protozoa have symbiont-bearing individuals in their midst. To reinforce this picture of the diversity of extrachromosomal systems, the next chapter lists some miscellaneous examples of extranuclear inheritance which have not yet been associated with a known organelle or with a defined physical agent such as a virus. These examples include various incompatibility phenomena in fungi, cytoplasmic supressors in yeast, cytoplasmic male sterility in plants, and various features of nucleocytoplasmic interaction in protozoa.

The final chapter briefly surveys the main arguments and discusses various theories of organelle evolution, the origin of eukaryotes, and their relationship to prokaryotes. There is a manageable well-selected reference list and a brief subject index. In general, Extranuclear Inheritance is a most useful monograph that should stimulate awareness of many interesting, important, and neglected phenomena in cell biology, and should help us see the genetic role of the nucleus in its proper perspective.

The third book to be discussed in this section is The Phylogeny of Human Chromosomes by H. N. Semlnez. Age-old problems can be looked at with gleaming new tools-part of the fascination of this stimulating little book is to see how modern cytological and biochemical techniques have been brought to bear on the problem of the origin of human chromosomes and hence to the fundamental question: whence came man? The first section of the book deals directly with the question of the origin of man, surveying the fossil record and presenting current views on the classification of the Hominoidea. According to Goodman (1975), the reader may be pleased to know, he or she belongs to the population of living beings classified under Homo sapiens, belonging to the superfamily Hominoidea, the family Hominidae, and the subfamily Homininae. In our subfamily are included the chimpanzee and the gorilla.

The next section deals with cytotaxonomy and the evolution of man and the great apes. Their chromosomes are compared in detail, both in number and also via the various banding methods (e.g., G-, R-, and Q-banding). There is a detailed account of chromosomal aberrations (heteromorphisms) in man and the great apes and also of chromosomal rearrangements by inversion and tel om eric fusion. From this analysis one can suggest an ancestral chromosomal complement of the Hominidae, details of which are given. The section ends with a short account of the relationship between speciation and chromosomal rearrangement.

The third and largest section is oriented toward biochemistry and molecular biology and deals with topics such as DNA sequence studies, satellite DNAs, palindromes, DNA replication, eu- and heterochromatin, and so forth. The new approaches have increased our understanding of the chromosome in molecular terms, as distinct from the more "bulk" morphological and staining


studies of classic chromosomology. It is difficult to tell from Seuanez's account, however, to what extent the new techniques have solved the problem of man's origin. One has the impression that the new methods have often merely raised new and more complicated questions. This is perhaps best summed up by a direct quotation from the last paragraph of the book:

... I feel it is necessary to emphasize how far we still are from having a clear idea of how our own species evolved. With the development of new techniques in the years to come let us hope that substantial information will be obtained which will enlarge the limited understanding we already have of our own nature and origins. Until then, and perhaps even then, the basic question of What is man? will remain still unanswered.

There is little doubt that The Phylogeny of Human Chromosomes is a most useful tool in the pursuit of the answer to this intriguing question.

3. MUSCLE AND Ca2+ TRANSPORT

Recent years have shown an increasing appreciation of the role of CaH in muscle function and it is therefore appropriate to discuss books on muscle and on CaH transport in the same section.

Smooth Muscle edited by E. Biilbring and T. B. Bolton is a part of Volume 35 of the British Medical Bulletin and is directed mainly at "physiologists, pharmacologists, and clinical pharmacologists." Nevertheless, much of the material in it would certainly be of interest to readers of SUBCELLULAR BIOCHEMISTRY. The first article by G. Gabella discusses smooth muscle cell junctions and the structural organization of smooth muscle in relation to its contractile ability. He deals with all aspects of smooth muscle organization, including the intercellular materials (collagen, elastin, and possibly mucopolysaccharides), the arrangements of the dense bands, small cell membrane invaginations called caveolae, intermediate junctions, gap junctions (nexuses), links between cells, and the intercellular material and, finally, the physical arrangement of myofilaments. The article, although only five pages long, is an excellent survey of the mean features of the organization of smooth muscle.

S. V. Perry and R. J. Grand then survey what is known of the biochemistry of smooth muscle contraction. They discuss our knowledge of contractile proteins in smooth muscle and deal with other constituents, such as dense bodies, 10-nm filaments, a-actinin, the M protein, and filamin. They also discuss the regulatory systems of smooth muscle (including the role of troponinlike systems, myosin phosphorylation, and calmodulin), as well as the contractile process. The authors compare the state of our knowledge of smooth muscle biochemistry with that of skeletal muscle. A. F. Brading then discusses the maintenance of the ionic composition of smooth muscle and gives an account


of the Na-K pump, Na-linked ion movements, and the regulation of Ca2+ and Cl- levels. A model for Na + exchange is presented, and this is discussed in relation to calcium movements, plasma membrane vesicles, and the general functioning of the sarcoplasmic reticulum.

Other chapters in Smooth Muscle deal with various aspects of membrane physiology, blood supply, innervation, peristalsis, drug receptors, cholinergic and adrenergic mechanisms, as well as the mode of action of prostaglandins. In their introduction, the editors survey the achievements of recent research in the subject, but also stress the outstanding problems. Many of these arise from the fact that there appear to be considerable differences in the properties of smooth muscle depending on where it occurs. There is clearly much work to be done in this field, with many of the tools successfully fashioned in the investigation of skeletal muscle. This publication makes a useful contribution to such an endeavor by bringing together under one cover specialized chapters of manageable size that cover all the major aspects of smooth muscle structure and function.

Calcium Transport and Cell Function, edited by A. Scarpa and E. Carafoli, is a large tome running to morc than 650 pages. It consists of the published proceedings of a conference of the same title held by the New York Academy of Sciences in late 1977. As there are nearly 60 papers in the book, plus a report of the discussion that followed, it is not possible to give an account of each topic covered. Instead, the main sections of the book will be surveyed and some papers of particular relevance to cell biochemistry discussed in a little greater detail.

The book begins with some introductory remarks by A. Scarpa and with an account by D. W. Urry of the basic chemistry of calcium and of its interaction with membranes. Part I then deals specifically with the measurement of calcium and includes accounts of microprobe X-ray analysis of calcium, calcium-sensitive electrodes, the use of photoproteins such as aequorin and obelin, metallochrome indicators, and finally "Extended X-ray Absorption Fine Structure" (EXAFS) studies. One is struck by the range and sophisti,cation of techniques now available for the study of calcium in biological systems-it is an interesting question as to whether our present appreciation of the central importance of calcium in biology is a result of the development of these techniques, or vice versa.

The next part deals with the interaction of calcium with subcellular organelles. H. J. Schatzmann and H. BUrgin begin with an account of calcium in human red blood cells, which includes a detailed discussion of the Ca-pump ATPase. A. N. Martonosi, T. L. Chyn, and A. Schibeci then give a short survey of calcium translocation in the sarcoplasmic reticulum and present a hypothesis for the regulation of the synthesis of Ca2+ ATPase mRNA by nuclear repressor proteins with a high affinity for Ca2+. A. L. Lehninger, B.


Reynafarje, A. Vercesi, and W. P. Tew then discuss the transport and accumulation of calcium in mitochondria. They give an account of high-affinity Ca2+ binding sites and of the possible participation of phosphocitrate in the storage of calcium phosphate in mitochondria. L. Moore and I. Pastan then describe energy-dependent calcium uptake in fibroblast microsomal fractions and discuss the interaction of calcium pumps in the plasma membrane, mitochondria, and endoplasmic reticulum. M. P. Blaustein, R. W. Ratzlaff, and N. K. Kendrick, then give an account of intracellular calcium regulation in presynaptic nerve terminals and survey the properties of nonmitochondrial A TP-dependent calcium storage systems in disrupted nerve terminals.

After Part II there is a report of a panel discussion on the previous two parts and this includes several contributions on the sarcoplasmic reticulum in relation to calcium metabolism and on mitochondrial transport, accumulation, and storage of calcium. Part III deals with the regulation of intracellular calcium and includes accounts of regulation in giant axons, mitochondria, and barnacle muscle fibers, as well as discussion of the role of calcium in inter- and intracellular communication.

Part IV discusses the hormonal control of calcium metabolism and includes an account of the action of the widely used ionophore A23187. There follows a panel discussion on Parts III and IV, which includes papers on the calcium channel in the sarcoplasmic reticulum, calcium transport in bone and intestinal cells, the physiological regulation of calcium metabolism, and the role of prostaglandins. The next part deals specifically with the role of calcium in muscle contraction and the final part is concerned with calcium in vision and secretion. The final panel discussion includes some more material on muscle action, vision and the role of calcium in secretion.

As may be judged from the above account, research into calcium now touches on a very wide range of fundamental biological processes. Calcium Transport and Cell Function therefore does a useful service in bringing together under one cover a representative sample of current experimental approaches to the topic. The book demonstrates the range of sophisticated techniques now being used and is a useful source of reference for those wishing to enter this rapidly expanding field of research.

4. GENERAL BIOCHEMISTRY

The next three books to be discussed (by J. W. Suttie, R. C. Bohinski, and D. E. Metzler, respectively) are all educational texts and illustrate the various approaches that may be adopted to the teaching of general biochemistry.

Introduction to Biochemistry, by J. W. Suttie, is an introductory text


designed around a one-semester elementary biochemistry course taught at the University of Wisconsin. The author has been careful to restrict the amount of material in the book to that which a student can reasonably be expected to assimilate in one semester. The main division of the book is into (1) The Chemistry of Biological Material, (2) Dynamics and Energetics of Biochemical Systems, (3) Energy Production in Biochemical Systems, (4) Energy Utilization in Biochemical Systems, and (5) Metabolic Control. After an account of pH and buffers, the main features of cell structure are presented, and this is followed systematically by chapters on carbohydrate, lipid, protein, and nucleic acid chemistry. An account of the structure and function of enzymes is followed by a chapter on biochemical energetics. A description of methods for studying intermediary metabolism is then followed, equally logically, by chapters on carbohydrate, lipid, protein, and nucleotide metabolism and on the tricarboxylic acid cycle. The section on energy utilization has chapters on photosynthesis, and the biosynthesis of carbohydrates, lipids, and nitrogencontaining compounds, including nucleic acids. The last part surveys the major metabolic pathways and discusses the various ways in which metabolism is controlled.

The student is thus led systematically through the subject and the text is well illustrated with clear diagrams, set problems and short reading lists. The book is clearly a well-thought-out and thoroughly tested teaching text and one would be surprised if students had serious difficulties with it. In contrast to Dyson's books discussed above (which one may call "cell orientated"), Introduction to Biochemistry belongs to the genre of what, for lack of a suitable term, may be called "Carbohydrate-Lipid-Protein-Nucleic Acid (CLPN) orientated" texts. In such books, the student is first asked to divide living matter into these four great chemical subdivisions and is then systematically taught their structure, how they are degraded, and how they are synthesized. The usual cement that binds together the four categories is bioenergetics. In such texts, cell organization is generally included as a subsection of one of the parts and is not treated as the core of the subject. Only the future will tell us whether the cell-structure-orientated or CLPN-orientated approaches are more fruitful-certainly Suttie's well planned book is an excellent example of the latter approach.

Modern Concepts of Biochemistry, by R. C. Bobinski, is a larger text. It may be used for one-semester courses, but it has sufficient material for use in longer courses. After an interesting introduction in which the author marks out the great range of studies included under the simple term "biochemistry" and also includes some salutory philosophy about the complexity of life, the first chapter deals with cellular organization; the structure of the major organelles is surveyed. There then follows a chapter on methodology, and this is followed by a treatment of pH, buffers, hydrogen bonding, and hydrophilic interactions.


Three chapters follow on amino acids and peptides, proteins, and enzymes, respectively, after which follows an account of nucleotide and nucleic acid chemistry and RNA, DNA, and protein biosynthesis. Carbohydrates, lipids, and biomembranes are then discussed, and this leads on to chapters on the citric acid cycle, oxidative phosphorylation, and photosynthesis. The last two chapters deal with lipid metabolism and the metabolism of nitrogen-containing compounds, and the book is completed with appendixes on isoenzymes in clinical diagnosis and on human genetic disorders.

Each chapter is richly amplified with diagrams, structural formulas, tables of data, and literature guides. The general impression is of a most readable and well-thought-out text. Although concepts are presented wherever possible, parts of the book are rather replete with factual material. For example, there is a full-page diagram of the metabolic pathways for squalene biosynthesis, and some students may have difficulty in deciding what is essential and what is merely reference material. Nevertheless Bohinski's book is an excellent attempt to reveal a unifying thread in biochemistry and to deal with the manifold problems associated with teaching a subject that is in a phase of rapid change and development.

The third of the educational texts considered here, Biochemistry: The Chemical Reactions of Living Cells, by D. E. Metzler, stands in a class of its own. The aim of the book is best explained by a direct quotation from the preface:

... rather than dividing biochemistry into segments centered around specific chemical compounds such as proteins, nucleic acids, lipids and carbohydrates, I treat chemical reactions of cells as a primary theme. While stressing biological concerns, I try to trace all physiological phenomena back to the underlying chemistry.

The book therefore stands at the opposite pole to those by Dyson discussed above. Instead of examining living processes as a function of cellular organization, they are looked on as the product of highly specialized, integrated, and spatially organized chemical reactions. A cursory inspection of the contents of the book shows how cleverly the author has organized his material in pursuit of this aim. Clearly, the "chemocentric" analysis of cellular function is a most rewarding exercise. Nevertheless there is a nagging doubt in the reviewer's mind as to whether such an analysis, even in full and minute detail, will provide us with a satisfactory answer to many of the current problems of cell biology. Is the cell merely a complicated machine made up of thousands of chemically interlocking parts, or has it some higher properties, not necessarily predictable from a knowledge of these parts?

Metzler's book is on a much larger scale than the two books just discussed, running to more than 1100 pages. Because of the originality of the author's approach, the main chapter divisions bear no relationship to the classical layout


of so many biochemical textbooks. The author first sets "The Scene of Action." This includes an account of the main features of prokaryotic and eukaryotic cell structure and of the evolution of complex organisms. The next chapter begins with a discussion of the structure of small molecules and leads on to an account of the chemistry of amino acids, proteins, mono- and polysaccharides, nucleic acids, and lipids. The chapter includes a discussion on ions of biological importance and of studies on the chemical composition of cells. There is then a detailed treatment of the energetics of biochemical reactions and this leads to a discussion of the forces that act between molecules of biological importance. There is also an account of the self assembly of complex macromolecular systems, including bacteriophage.

"Membranes and Cell Coats" is the title of the next chapter in which the structure and function of a wide range of biomembranes are surveyed. Enzymes are then discussed, and a full account is given of enzyme kinetics, the various proposed mechanisms for enzyme action, and the regulation of enzyme activity. The next chapter surveys the types of reaction catalyzed by enzymes, classifying these reactions in strictly chemical terms. Coenzyme structure and mode of action are then discussed and this leads onto an account of the "organization of metabolism." Catabolic pathways are described first; then there is an account of electron transport and oxidative phosphorylation, plus a description of various oxygenases and hydroxylases. Biosynthesis is discussed in a generalized manner (i.e., "How molecules are put together"), and there follows a chapter on some selected specific pathways in carbohydrate and lipid metabolism.

Typical of the originality of the author's approach, and of the way he has tried to break out of the straitjacket of conventional texts, is the fact that the treatment of photosynthesis is included in a more general chapter entitled "Light in Biology." This includes an account of the electromagnetic spectrum, circular dichroism, optical rotatory dispersion, fluorescence, phosphorescence, and the biochemical processes of vision. Thus the reactions of photosynthesis are perceived by the student as a special case of the more general problem of the interaction of biological molecules with the whole spectrum of electromagnetic radiation. There is a chapter on the metabolism of nitrogen-containing compounds followed by one on biochemical genetics, nucleic acid synthesis, and protein synthesis. The final chapter is on growth, differentiation, and chemical communication between cells.

An original feature of the book is the inclusion of special "boxes" interspersed throughout the text, and printed over a green background. These are not chapter synopses, but contain ancillary material on topics such as vitamins, essential elements, metabolic diseases, antibiotics, and physiological chemistry. By choosing appropriate patterns of boxes, as suggested by the author, students studying special aspects of biochemistry can amplify the main material in the


text proper with the details in the boxes. The nonspecialist student aiming at a fundamental treatment of the subject can ignore the boxes altogether. The text has a high standard of presentation, and each chapter includes useful references and a series of helpful study questions. The book includes an appendix on the construction of molecular models as well as a detailed and fully comprehensive subject index.

Biochemistry: The Chemical Reactions of Living Cells is thus an original and stimulating textbook. Anyone who has taken the trouble to work through it systematically would have a fundamental understanding of the chemical reactions that occur in living systems. The originality in the way the material has been arranged should also help break down artificial barriers between different parts of the subject and demonstrate that all biological processes have a common underlying theme that is derivable from the chemical properties of the various interacting molecular species that make up living matter. There is thus no doubt that Metzler's book is a most significant contribution to the educational biochemical literature.

D.B.R.

Index

Acetabularia, primary pre-rRNA, 18 Acheta domestic us

extrachromosomal rRNA genes, 5 rRNA genes, 19

Acid phenylphosphatase, in thyroid subcellular fractions, 242

Acid phosphatase, in thyroid subcellular fractions, 224

Actinomycin D, effect on synthesis of ribosomal proteins, 52

Adenylate cyclase in thyroid plasma membranes, 219, 246 TSH-sensitive, 249

A granules, in thyroid epithelial cells, 150 Albumin

biosynthesis, and catalase biosynthesis. 202

in hepatoma, 127 secretion, 119

Alcohol, effect on polysome binding, 126 Alkaline phosphatase, in thyroid subcellular

fractions, 222 a-Amanitin, effect on mRNA synthesis, 50 Aminoacyl tRNA, binding to A site of

peptidyl transferase, 16 Amphibia, rRNA gene amplification, 5 Antibody absorption, in spheroplasts, 312 Antigens

as markers, 216 in Micrococcus lysodeikticus membranes,

353-365 Antiserum, to NADH dehydrogenase, 278 Anucleolate mutants, in Xenopus laevis, 9 Ascites cells, pre-rRNA secondary structure,

33 A site, rRNA-tRNA binding, 16 A-T base pairs, in 5 S rRNA, 14

ATPase antigens, 362 latency, role of f subunit, 342 in Micrococcus lysodeikticus membranes,

336-352 fine structure, 337

in mitochondrial stalked bodies, 334 in Streptococcus faecaUs membranes, 336 in thyroid subcellular fractions, 222

Azidodibenzofuran, effect on NADH dehydrogenase, 292

Bacillus megaterium, effect of lysozyme, 313 Bacillus stearothermophilus, stalked bodies,

337 Bacillus subtiUs. "peri plasmic" protein and

fatty acid exchange, 331 Bacterial membranes

freeze fracture studies, 318 plasma membrane function, 310 ultrastructure, 312-319

Benzidine, peroxidase substrate, 233 B granules, in thyroid epithelial cells,

150 Bilayer model, asymmetry, 356 Biogenesis

of eukaryotic ribosomes major stages, 45 posttranscriptional control, 51-58 regulation, 44-58 review literature, 1 transcriptional control, 57-58

of glyoxysomes, 171-203 of peroxisomes, 171-203

Blobel and Sabatini, 144 Branched-chain fatty acids, in Micrococcus

lysodeikticus membranes, 328

395

396

Capsular polysaccharides, immunology, 353 Carcinogenesis, changes in endoplasmic

reticulum, 124 Carcinogens, binding to

cytosol, 124 microsomes, 124 mitochondria, 124 nuclei, 124

Cardiolipin biosynthesis, 330

inhibition by Micrococcus Iysodeikticus mesosomes, 330

in bovine heart mitochondria, 243 mitochondrial marker, 227 role in cytochrome oxidase activity, 295 role in NAOH dehydrogenase activity, 295 synthetase, release from Micrococcus

leisodeikticus. 318 Cartenoids, in Micrococcus Iysodeikticus

plasma membrane, 320 Castor bean endosperm, glyoxysomal mRNA,

187 Castor oil plant, triglycerides, 184 Catalase

biosynthesis, 186 absence of molecular weight changes, 202 and albumin synthesis, 202

in Micrococcus Iysodeikticus cytosol, 365 in peroxisomes, 174 in thyroid subcellular fractions, 225

Cell cycle immunoglobulin biosynthesis, 154 number of rRNA genes, 46

Cell surface glycoproteins, 367 Salmonella typhimurium. 358

Cell wall polymers, biosynthesis, 281 effect of penicillin, 281 in Micrococcus Iysodeikticus. 281-285

Chaotropic agents, effect on hydrophobic interactions, 281 multisubunit enzymes, 280, 281 NAOH dehydrogenase, 272

Chloroplastal ONA, coding for large subunit of ribulose diphosphate carboxylase, 196

Chloroplasts, biogenesis, 196 Cholesterol

in endoplasmic reticulum, 225 in thyroid plasma membranes, 219

Chromatophores, Rhodopseudomonas sphaeroides. 312

Index

Chromophores, in NAOH dehydrogenase, 290

Clofibrate, and peroxisome proliferation, 178 Cloning, 5 S rONA, 31 Clustering, rRNA genes, 3, 4 Colicin E3, effect on protein synthesis, 95 Collagen

effect of prohydroxylase, 146 synthesis by bound polysomes, 127

Colymbetesfuscus. extrachromosomal rRNA genes, 5

Compartmentalization, endoplasmic reticulum, 149-151

Complex I, 268 discontinuous gel electrophoresis, 275 effect of cholate, 296 effect of phospholipase A, 296 epr spectrum, 269

possible effects of denaturation, 271 lipid replacement studies, 294 SOS-polyacrylamide gel electrophoresis,

272 steady state kinetics, 270

Concanavalin A, and Micrococcus Iysodeikticus antigens, 359

Condensing vacuoles, 118 Conformation, rRNA, 13,82 Coomassie Blue stain, NAOH dehydrogenase

subunits, 276 Cooperative effects, in ribosome

reconstitution, 98 Core glycosylation, 193 Cotranslational processes, 193 Crossed immunoelectrophoresis, 353

of NAOH dehydrogenase from M. Iysodeikticus. 365

and SOS gel electrophoresis, 354 Cycloheximide

effect on protein synthesis, 50 and nucleolar RNA polymerase turnover,

49 Cytochrome a" in Micrococcus

Iysodeikticus. 331 Cytochrome b. in Micrococcus Iysodeikticus.

331 Cytochrome b l , in Micrococcus Iysodeikticus.

331 Cytochrome b" biosynthesis, 193

Index

Cytochrome c, in Micrococcus lysodeikticus, 331

Cytochrome oxidase role of cardiolipin, 295 in thyroid subcellular fractions, 219

latency, 217 Cytochrome P-450, in endoplasmic reticulum,

122 Cytosol

carcinogen binding, 124 ribosome migration, 57 thyroid lactate dehydrogenase, 221

D-Alanine carboxypeptidase, and UDP-muramylpentapeptide, 324

"Dangling" messenger, 141 Danielli and Davson model, 358 Do-Carboxypeptidase, 320

in Micrococcus lysodeikticus, 320 Dehydrogenases, in M. lysodeikticus plasma

membranes, 320 Deoxyribonuclease, from thyroid, 217 Diazobenzene sulfonate, labeling of NADH

dehydrogenase, 324 Differential pelleting, thyroid homogenates,

218-222 Differential replication, rRNA genes, 16 Dimyristoyl lecithin, and complex I, 294 Di-Na-phenylphosphatase, from thyroid,

217 Diphenyl iodonium, and NADH

dehydrogenase, 290 Diphtheria toxin, membrane transport, 197 Discontinuous gel electrophoresis, 275 Dithionite, reduction of NADH

dehydrogenase chromophores, 281 "Domains," in ribosomal subunits, 86

RNA-protein interactions, 87 Drosophila, plasmid rRNA genes, 30 Drosophila melanogaster

rRNA genes, 8 5 S rRNA, 14

Dytiscus marginalis, rRNA genes, 19 extrachromosomal, 5

EDTA, and membrane-ribosome interactions, 13 7

Electron shuttles, role of peroxisomes, 177 Electron transport chain, in Micrococcus

lysodeikticus. 331-334

Endonucleases action on pre-rRNA, 35 in nucleoli, 42

Endoplasmic reticulum changes during carcinogenesis, 124 cholesterol content, 225 cisternae, 117 compartmentalization, 149-151

397

continuity of rough with smooth, 123 continuity with peroxisomal membrane, 189 cytochrome P-450, 122 functional aspects, 121-125 glucose-6-phosphatase, 228 integral proteins, 129 lipoprotein globules, 120 luminal face, 129 membrane composition and structure, 119-

121 membrane symmetry, 120 "microenvironments," 148 monooxygenase, effect of drugs, 123 mRNA binding, 148 NADH-cytochrome P-450 reductase, 122 peripheral proteins, 129 phospholipid synthesis, 188 posttranslational modifications, 149-151 protein synthesis, 125-137

compartmentalization, 149-151 ratio of smooth to rough, 122 role in protein synthesis, 117-155

Enzymes, as markers, 216 epr spectroscopy, NADH dehydrogenase, 269 Escherichia coli

cardiolipin biosynthesis, 330 Fo-F,-ATPase complex, 351 membrane vesicles, 362 ribosomes, 81-104 23 S rRNA, nucleotide sequence, 83 transport, 362

Ethionine, effect on polysome spirals, 141 Etiolated leaves, peroxisomes, 186 Eukaryotes

gene expression, 59 RNA polymerases, 16

Eukaryotic ribosomes biogenesis, 213-251

posttranscriptional control, 51-58 regulation, 44-58 review literature, 1 transcriptional control, 46-51

398

Eukaryotic ribosomes (cont.) preribosomes, processing, 31-44 pre-rRNA

processing, 31-44 structure, 32-33

ribosomal genes, 2-16 differential replication, 16 transcription, 16-31

in vitro, 29-31 5 S rRNA genes, 12-14

Evolution of L-rRNA sequences, 32 of rRNA terminal nucleotides, 40 of S-rRNA sequences, 32

Exonucleases, action on pre-rRNA, 35 Extrachromosomal rRNA genes, 5

F.-ATPase, in Escherichia coli, 351 F.-F1-ATPase complex, in Escherichia coli,

351 F1-ATPase

biosynthesis, 280 in Escherichia coli

mutants, 351 reconstitution, 350

~ subunit, 342 latency, 349 in Micrococcus Iysodeikticus, 346

cytoplasmic face of plasma membrane, 340

membrane location, 336-352 molecular weight, 347 possible glycosylation, 348 proteolytic degradation, 342 subunit composition, 347

10-nm particles, 319 reconstitution in E. coli, 350 in Salmonella typhimurium, subunit

composition, 349 Fatty seeds, glyoxysomes, 184-185

proliferation, 187 Ferritin-antibody labeling, lipotechoic acids,

358 Flavoprotein core, NADH dehydrogenase,

302 Flavoprotein fragments

in complex I, 273 in NADH dehydrogenase, 302

"Flip-flop," monolayer phospholipids, 189 5-Fiuoroorotate, and mRNA biosynthesis, 53

Index

FMN, in NADH dehydrogenase, 269 Free ribosomes, effect of partial hepatectomy,

126 Freeze-fracture

bacterial membranes, 318 mesosomes, 319

Galactosyltransferase, in thyroid subcellular fractions, 221, 243

GDP-mannose, and lipomannan biosynthesis, 327

Gel filtration, thyroid homogenates, 218 Gene expression, eukaryotic ribosome

biogenesis model, 59 Gene-spreading technique, 26 Gluconeogenesis, and glucose-6-phosphatase,

228 Glucose-6-phosphatase, in thyroid subcellular

fractions, 228 correction by phenyl phosphatase, 229 nuclear activity, 229

~-Glucuronidase, in thyroid subcellular fractions, 218

latency, 217 Glutamate dehydrogenase, synthesis by

membrane-bound polysomes, 135 ~-Glycerophosphatase, in thyroid subcellular

fractions, 217 Glycoprotein G, in vesicular stomatitis virus

(VSV),I92 Glycoproteins

in lysosomes, 149 in mitochondria, 149 oligosaccharide patterns, 150 synthesis in rough endoplasmic reticulum,

193 Glycosylation

at polysome level, 152 of secretory proteins, 128 of vesicular stomatitis virus protein, 192

Glycosyltransferases in Golgi apparatus, 199 membrane-bound, 150

Glyoxylate cycle, in glyoxysomes, 173 Glyoxysomes

biochemical constitution, 173 biogenesis, 171-203 from fatty seeds

biochemistry, 184-185 proliferation, 187

Index

Glyoxysomes (cont.) glyoxylate cycle, 173, 185 isocitrate lyase, 185 malate dehydrogenase biosynthesis, 203 malate synthase, 185 membranes

alkaline lipase, 198 cytochrome bs, 198 N-demethylases, 198 hydroxylases, 198 polypeptide composition, 199 similarity to endoplasmic reticulum, 199

morphology, 172-174 mRNAs, 187 .a-oxidation pathway, 173 proximity to spherosomes, 184 topographic relationships, 172-174

Golgi apparatus, 118 glycosyl transferases, 150 and protein glycosylation, 199 proteins, site of synthesis, 136 from thyroid, 243-244

separation from plasma membrane, 243 Gradient centrifugation, thyroid

homogenates, 221-227 Gram-negative organisms

freeze-fracture studies, 318 outer membrane, 311 plasma membrane, 311

Gram-positive organisms, freeze-fracture studies, 318

Guaiacol, peroxidase substrate, 233 Guaiacol peroxidase

effect of heparin on sedimentation, 233 in thyroid rough endoplasmic reticulum,

233

~+-ATPase, in Micrococcus Iysodeikticus, 352

Heparin and peroxidase sedimentation, 233 and thyroid rough endoplasmic reticulum,

225 Hepatoma, albumin synthesis, 127 Heteroduplex mapping, 10 Heterogeneity, rough endoplasmic reticulum,

151 Histone mRNA, 143 Histones, and transcribed rDNA, 23 HnRNA, biosynthesis, 52

Homogenization, thyroid tissue, 214 get filtration of homogenates, 218

399

Human chromosomes, rRNA gene clusters, 4 Hydrophilic probes, NADH dehydrogenase

labeling, 282-284 Hydrophobic interactions, in NADH

dehydrogenase, 281,285,286 Hypertrophic thyroid, nuclear lipids, 240

Immunoelectron microscopy, ribosomal proteins, 10, 101

Immunoelectrophoresis crossed two-dimensional, 353 of Micrococcus Iysodeikticus membranes,

345 of succinylated lipomannan, 346

Immunoglobin secretion, 119 Immunoglobulin, light chain biosynthesis,

152 Initiation complex, 96 Initiation factor IF-3

effect on ribosomal proteins, 99 interaction with 16 S rRNA, 98

Initiation of protein synthesis, effect of Verrucarin A, 147

Insects, rRNA gene amplification, 5 Insulin secretion, 119 Intermediate pre-rRNA, 37 Introns, in rRNA genes, 8 Iodonaphylazide

labeling of NADH dehydrogenase, 285 [ 12SIl peroxidase, labeling of membranes, 366 Iron-protein fragment

in complex I, 273 in NADH dehydrogenase, transmembrane

organization, 299 Iron-sulfur groups, in NADH

dehydrogenase, 271 Isocitrate dehydrogenase, in Micrococcus

Iysodeikticus cytosol, 365 Isoelectric points, NADH dehydrogenase

subunit polypeptides, 281, 282

Kethoxal, action on 16 S rRNA, 16 Kidney glycoproteins, synthesis by bound

polysomes, 127

Lactate dehydrogenase, in thyroid cytosol, 221

Lactobacilli, lysoteichoic acids, 358

400

Lactoperoxidase iodination, NADH dehydrogenase, 283

Laser light scattering, rRNA studies, 85 Latency, F1-ATPase, 342 Leaf peroxisomes, 181-183

proliferation, 186-187 Light chain immunoglobulin

biosynthesis in plasmacytoma, 152 in cell cycle, 154

Lipases, in spherosomes, 187 Lipid biosynthesis, in Micrococcus

lysodeikticus membranes, 328-331 Lipid depletion, NADH dehydrogenase

studies, 294 Lipid-protein interactions, in NADH

dehydrogenase, 292-298 Lipids

in hypertrophic thyroid nuclei, 240 in succinate dehydrogenase, 332 in thyroid mitochondria, 241 in thyroid nuclei, 240

Lipid transport in membranes, 191 Lipolytic enzymes, in thyroid subcellular

fractions, 234-238 Lipomannan biosynthesis

in Micrococcus lysodeikticus, 325-327 mesosomes,322

role of GDP-mannose, 327 Lipopolysaccharides

immunology, 353 localization in Salmonella typhimurium,

358 Lipoprotein globules, in endoplasmic

reticulum, 120 Lipoteichoic acids, ferritin-antibody labeling,

358 Liver peroxisomes

biochemical properties, 181-183 proliferation, 185-186

Long-Acting Thyroid Stimulator (LATS) Inhibitor, 247

L-rRNA evolution, 32 genes, 2 intermediate pre-rRNA, 37 in nucleolus, 58 segment in primary pre-rRNA, 29

Lymphocytes, effect of phytohaemagglutinins, 55

Lysophospholipase, in thyroid, 231

Lysosomes gl ycoproteins, 149 thyroglobulin hydrolysis, 214 from thyroid, 241, 242

heterogeneity, 224 hydrolases, 217 mitochondrial contamination, 219

Lysostaphin, effect on Staphylococcus aureus, 313

Lysozyme

Index

effect on Bacillus megaterium strain KM, 313 effect on Micrococcus lysodeikticus, 309

Malate dehydrogenase, biosynthesis glyoxysomal enzyme, 203 role of membrane-bound polysomes, 135

Mammary gland milk proteins, synthesis by membrane-bound polysomes, 127

Mannan biosynthesis, 326 in Micrococcus lysodeikticus, 325

Mannobiosyldiglyceride, in Micrococcus lysodeikticus, 327

Mannosaminuronic acid polysaccharide, 322 Mannosyl-I-phosphoryl undecaprenol, role in

mannan biosynthesis, 326 Mannosyl transferase, in thyroid subcellular

fractions, 221 Marker enzymes, in thyroid, 216-218 Matrix proteins, in microbodies, 197

site of biosynthesis, 194 Matrix units, in rDNA, 21 Maturation

of pre-rRNA, 34-42 of primary preribosomes, 59

Meiotic recombination, and nontranscribed sequences, 15

Membrane-bound ribosomes in brain cortex cells, 136 in choroidal epithelial cells, 136 cytochrome b, biosynthesis, 193 in differentiating muscle, 136 effect of alcohol administration, 126 nascent collagen polypeptides, 146 synthesis of

catalase, 186 cytosolic enzymes, 128 glutamate dehydrogenase, 135 malate dehydrogenase, 135 mitochondrial proteins, 135

Index

Membrane flow hypothesis, 190 and microbody membrane biogenesis, 201

Membrane lipids, in microbodies, 188-191 Membrane potential, in Micrococcus

lysodeikticus membranes, 334 Membranes

asymmetry, 190,356 bacterial,312-320 from endoplasmic reticulum, 118-125

composition and structure, 119-121 from erythrocytes, 132 from Micrococcus lysodeikticus, 320-352 interaction with

mRNA, 147-148 nascent polypeptides, 143-147 polysomes, 137-148 60 S ribosome subunit, 137-143

labeling by [12SIjperoxidase, 366 lipid transport, 191 peroxisoinal, lipid composition, 198 proteases, 13 2 proteins

in microbodies, 191-193 in reticulocytes, 133 transfer and "signal" hypothesis, 144

symmetry, 120 thyroid,238-251 vesicular stomatitis virus (VSV),

biogenesis, 191 Membrane transport, diphtheria toxin, 197 Membrane vesicles, 214, 362 Menaquinones

in Micrococcus lysodeikticus membranes, 320

in Mycobacterium ph lei, 333 Mesosomes

artifactual nature, 319 fatty-acid exchange with plasma

membrane, 331 freeze-fracture studies, 319 membranes, 313

Methylation, of pre-rRNA, 32 Microbodies

dimensions, 172 matrix, 172 matrix proteins

biosynthesis, 201-203 segregation, 197 site of synthesis, 194

Microbodies (cont.) membranes, 172

membrane flow, 201 models for biogenesis, 193-194 synthesis of

lipids, 188-191 proteins, 198-201

401

models of biosynthetic mechanisms, 187-197

proliferation, 185-187 proximity to endoplasmic reticulum, 174-

185 review literature, 171

Micrococcus flavius, lipomannan, 326 Micrococcus lysodeikticus

absence of lipoteichoic acids, 326 ATPase antigens, 362 ATPase staining, 337 cytoplasmic compartment

catalase, 365 isocitrate dehydrogenase, 365 polynucleotide phosphorylase, 365

Do-carboxypeptidase, 320 F,-ATPase

CaH stimulation, 346 localization in plasma membrane, 340 molecular weight estimates, 347 possible glycosylation, 348 proteolytic degradation, 342 subunit composition, 347

H+-ATPase, 352 history of research, 309 lipomannan, 326 mannan, 325 mannobiosyl diglyceride, 327 mannosaminuronic acid polysaccharide, 322 membranes

absence of phosphatidyl ethanolamine, 328

alcohol dehydrogenase, 332 antigenic architecture, 353-365 biochemical characterization, 320-352 cardiolipin localization, 363 coupling factor, 349-352 cytochromes a2, b, b" and c, 331 D-Iactate dehydrogenase, 332 EDT A shock washes, 318 electron transport chain, 331-334 enzymic distribution, 320-322 F,-ATPase, 336-358

402

Micrococcus lysodeikticus (cont.) fatty acid composition, 328 immunoelectrophoresis, 345 lipid biosynthesis, 328-331 lipomannan biosynthesis, 325-327 malate dehydrogenase, 332 NADH dehydrogenase, 332 10-nm particles, 319 phosphatidyl ethanolamine localization,

363 phosphatidyl glycerol localization, 363 release of cardiolipin synthetase, 318 release of NADH dehydrogenase, 318,

343 solubilization by Triton X-100, 355 succinate dehydrogenase, 332

mesosomes absence of respiratory enzymes, 356 distinction from plasma membranes,

313 inhibition of cardiolipin synthesis, 330 role in lipomannan biosynthesis, 322 succinylated lipomannan, 356

mucopeptide, 310 murein, 310 NADH dehydrogenase

crossed immunoelectrophoresis, 365 release from membranes, 343

nomenclature, 309 peptidoglycan, 310

metabolism, 323-325 plasma membrane

antigenic complexity, 353, 359 asymmetry of antigens, 359 carotenoids, 320 cytochromes, 320 D-alanine carboxypeptidase, 324 dehydrogenases, 320 distinction from mesosomal membranes,

313 general properties, 366 menaquinones, 320 phospholipids, 320

polymannose, 325 protoplasts, surface antigens, 359 respiratory chain

inhi bi tors, 334 membrane potential generation, 334

subfractionation, 320 release of Do-carboxypeptidase, 320

Micrococcus lysodeikticus (cont.) surface antigens, reactions with

concanavilin A, 359 surface profiles, 312 teichuronic acid, biosynthesis, 324 wall polymer biosynthesis, 323-325

Index

Micrococcus sodonensis. lipomannan, 326 Micronucleus, Tetrahymena pyriformis

rRNA genes, 6 Microsomal fraction

carcinogen binding, 124 thyroid, 229

Mitochondria carcinogen binding, 124 F,-A TPase biosynthesis, 280 glycoproteins, 149 inner membrane

ATPase, 336 NADH dehydrogenase organization, 268 stalked bodies, 336

protein synthesis, membrane-bound polysomes, 135

succinate dehydrogenase, 332 from thyroid, 241,242

cardiolipin content, 227 lipid composition, 241 lysosomal contamination, 219

from yeast, attached 80 S ribosomes, 195

Mitotic recombination, 15 Monolayers

phospholipid "flip-flop," 189 in thyroid nuclei, 241

Monooxygenase, in endoplasmic reticulum, 123

mRNA binding to endoplasmic reticulum, 148 for cytochrome b" 193 for glyoxysomal proteins, 187 for histone, 143 interaction with membranes, 147-148 recognition by ribosomes, 95 in rough endoplasmic reticulum, 151 segregation in rough endoplasmic

reticulum, 149 synthesis, effect of a-amanitin, 50 for thyroglobulin, 245 transfer from nucleus to cytoplasm, 148

Multisubunit enzymes, 281, 282 Muramidase, effect on streptococci, 313

Index

Mycobacterium phlei menaquinone, 333 NADH oxidation, 333

Myeloma cells histone mRNA, 143 60 S ribosomal subunits, 146

N-Acetylglucosaminyltransferases, in thyroid subcellular fractions, 243

N-Acetylhexosaminidase, in thyroid subcellular fractions, 242

NADH binding site in NADH dehydrogenase, 289 oxidation via peroxisomes, 177

NADH-cytochrome P-450 reductase, in endoplasmic reticulum, 122

NADH dehydrogenase alternative names, 268 binding site for NADH, 289 chromophores, 281, 290 discontinuous gel electrophoresis, 275 effect of chaotropic agents, 271 effect of cholate, 294 electron-carrying arm, 298 flavoprotein core, 302 flavoprotein fragment

NADH-ferricyanide oxidoreductase, 287 polypeptide composition, 273 surface covering, 302

FMN content, 269 fragmentation of enzyme, 271-272 functional unit, 269-271 gel electrophoresis, 272 hydrogen-carrying arm, 298 hydrophobic interactions, 281 iron-protein fragment, 273

redox potential, 290 transmembrane organization, 299

iron-sulfur groups, 271 isolation of pure enzyme, review literature,

267 labeling by diazobenzene sulfonate, 282 labeling by iodonaphthylazide, 285

effect of lipid depletion, 297 lactoperoxidase iodination, 283 lateral organization, 300-301 lipid depletion studies, 294

effect on iodonaphthylazide labeling, 297

lipid-protein interactions, 292-298

NADH dehydrogenase (cont.) membrane-bound enzyme, review

literature, 267

403

from Micrococcus lysodeikticus. crossed immunoelectrophoresis, 365

model of structure, 301-303 molecular organization, 267-303 NADH binding site, 289 paramagnetic species, 269 phospholipids, 292-298 polypeptide composition, 272-279 polypeptide isoelectric points, 281-282 protein components, 271-279 protein structure, 279-292 proteolytic digestion, 286-289 organization in membrane, 298-301 reaction with azidodibenzofuran, 292 reaction with diphenyliodonium, 290 reaction with ubiquinol-cytochrome c

oxidoreductase, 300 reduction by dithionite, 281 release from Micrococcus lysodeikticus

membranes, 318 review literature, 267 role of cardiolipin, 295 steady state kinetics, 270 structure/function relationships, 289-292 subunit components

Coomassie Blue staining, 276 coordinated antiserum precipitation, 278 labeling by diazobenzene sulfonate, 282 labeling by iodonaphthylazide, 285 polypeptides, 272-279 proteolytic digestion, 286

terminology, 268-269 transmembrane organization, 298-300 treatment with chaotropic agents, 272 ubiquinone reductase, effect of

phospholipid removal, 292 NADH-ferricyanide oxidoreductase, 287 NADH-ubiquinone oxidoreductase, 268 NADPH-cytochrome c reductase

in plasma membrane cytoplasmic face, 133 in thyroid nuclear fractions, 229

Nascent polypeptides, interaction with membranes, 143-147

Nectin, and ATPase attachment to membranes, 350

Neutron scattering, and rRNA packing, 99 Nitrogen cavitation, 248

404

10-nm particles, in Micrococcus Iysodeikticus membranes, 319

N', N'-dimethyladenosine, in 16 S rRNA, 103

Nonhistone proteins, and transcribed rDNA, 23

Nonribosomal proteins, and preribosomes, 44 Nontranscribed sequences

and recombination, 15 in rDNA, 21 in rRNA genes, 10

Nuclei carcinogen binding, 124 from Chinese hamster kidney cells, RNA

polymerase, 236 5 S rRNA synthesis, 31 from hypertrophic thyroid

chemical composition, 239 isopycnic density, 238

from thyroid, 238-241 chemical composition, 239 exogenous DNA and RNA polymerase,

236 glucose-6-phosphatase, 229 isolation techniques, 216 isopycnic density, 238 lipid composition, 240 NADPH-cytochrome c reductase, 229 peroxidase, 229

Nucleolus from L cells, endonucleases, 42 L-rRNA particles, 58 maturation of primary preribosome, 59 from Novikoff hepatoma, endonucleases, 42 and ribosome biogenesis, 60 ribosome migration, 57 RNA polymerase turnover, 49 45 S transcription products, 30

Nucleoplasm, ribosome migration, 57 Nucleosomes, unfolding, 24 5'-Nucleotidase, in thyroid subcellular

fractions, 222 Nucleotide precursors, in peptidoglycan

biosynthesis, 323 Nucleotides, effect on rRNA gene

transcription, 51 Nucleotide sequence, E. coli 23 S rRNA, 83 Nucleus

degradation of ribosomes, 55 rRNA wastage, 55

Index

Obligate aerobes, F1-ATPase latency, 349 Oligonucleotides, release from rRNA, 101 Organelles, thyroid, 238-251 tJ-Oxidation pathway, in glyoxysomes, 173

Palmitoyl coenzyme A, oxidation by peroxisomes, 179

Partial hepatectomy effect on free ribosomes, 126 effect on peroxisomes, 185

Penicillin, and bacterial cell-wall biosynthesis, 323

Peptidoglycans biosynthesis, 323 in Micrococcus Iysodeikticus, 323-325

Peptidyl transferase center, aminoacyl tRNA binding, 16

"Peri plasmic" protein, 331 Peroxidase

substrates, 233 in thyroid subcellular fractions, 232-234

nuclear activity, 229 Peroxisomes

biochemical properties, 174-185 biogenesis, 171-203 catalase

contribution to total peroxisomal protein, 174

site of synthesis, 186 effect of clofibrate, 178 effect of partial hepatectomy, 185 effect of tibric acid, 180 effect of Wy-14643, 180 fatty acid oxidation pathway, 118 from leaves

biochemical properties, 181-183 malate dehydrogenase, 182 ontogeny, 186 photorespiratory glycolate pathway, 182 proliferation, 186-187 urate oxidase, 182

from liver biochemical properties, 181-183 proliferation, 185-186

matrix proteins biosynthesis, 201-203 segregation, 197

membrane biogenesis models, 193-194 membrane lipid biosynthesis, 188-191,

197,198

Index

Peroxisomes (cont.) membranes, continuity with endoplasmic

reticulum, 189 lipid composition, 198 protein biosynthesis, 188-191, 198-201

morphology, 172-174 palmitoyl-CoA oxidation, 179 proliferation, 185-187 substrate-mediated electron shuttles, 177 topographical relationships, 172-174

Phosphatidylcholine in bovine heart mitochondria, 293 in peroxisomal membranes, 198

Phosphatidylethanolamine absence from Micrococcus lysodeikticus

membranes, 328 in bovine heart mitochondria, 293 in peroxisomal membranes, 198

Phosphatidylinositol, in peroxisomal membranes, 198

Phosphodiesterase, in thyroid, 217 Phospholipase, in thyroid, 231, 232 Phospholipid exchange proteins, 198 Phospholipids

biosynthesis, 188 "flip-flop," 189 in Micrococcus lysodeikticus membranes,

320 in NADH dehydrogenase, 267

role in ubiquinone reductase, 292 Photorespiration

effect of oxygen, 181 and photosynthesis, 181

Physarum polycephalum rONA matrix units, 21 r-chromatin, 18 5 S rRNA genes, 12

Plant leetins, membrane transport, 197 Plasmacytoma, immunoglobulin biosynthesis,

152 Plasma membrane

asymmetry, 120 bacterial, 310 cytoplasmic face, 133 in gram-negative bacteria, 311 in Micrococcus lysodeikticus

antigenic complexity, 353, 355 general properties, 366

NADPH-cytochrome c reductase, cytoplasmic face localization, 133

Plasma membrane (cont.) prokaryotic, 310

compared to eukaryotic, 367 proteins, site of biosynthesis, 136 reaction with agglutinins, 363 in thyroid, 245-251

adenylate cyclase, 246 contamination of isolated fractions,

246

405

heterogeneity of isolated fractions, 250 lipid content, 247 method of isolation, 245

Plasmids, with Drosophila rRNA genes, 30 Pleurodeles waltlii. rRNA genes, 19 Polyaldehydes, cross-linking of ribosomal

proteins, 11 Polymannose, in Micrococcus lysodeikticus.

325 Polynucleotide phosphorylase, in

Micrococcus lysodeikticus cytosol, 365

Polysome run off, 147 Polysomes

attachment via dangling messenger, 141 effect of alcohol administration, 126 effect of ethionine, 141 free, protein synthesis activity, 125-127 in Golgi fractions, 136 interactions with membranes, 137-148 membrane-bound

protein synthesis activity, 320-323 synthesis of secreted proteins, 323-

325 protein glycosylation, 152 from thyroid, 244, 245

Polytron homogenizer, 248 Posttranscriptional control, of ribosome

biogenesis, 57-58 Posttranslational modification, of proteins in

endoplasmic reticulum, 155 pppNp, in primary pre-rRNA, 28 pre-mRNA

effect of 5-fluoroorotate, 53 effeet of toyocamycin, 53

Preribosome intranuclear degradation, 55 nonribosomal proteins, 44 processing, 31-44 and structural ribosomal proteins, 52 structure, 293-296

406

Pre-rRNA action of nucleases, 35 denaturation spectra, 33 gel electrophoresis, 34 maturation pathways, 34-42 methylation, 342 processing, 31-44

intermediates, 37 and rRNA pools, 39 secondary structure, 32, 33 uridine to pseudouridine conversion, 32

Primary preribosome, maturation, 59 Primary pre-rRNA

heterogeneity, 27 pool composition, 27 pppNp content, 28 size variations, 18 termination signal, 29 use of gene-spreading technique, 26

Primary rONA transcript, 25 Proalbumin, 144 Proinsulin, 144 Prokaryote plasma membrane, 310 Prolyl hydroxylase, action on collagen, 146 Promoter signals, in rRNA genes, 13 Proteases, in membranes, 132 Protein binding sites, in E. coli rRNA, 94-

99 Protein glycosylation, and Golgi apparatus,

199 Protein-mediated lipid transport, 191 Protein synthesis

by free polysomes, 125-127 inihibition by colicin E3, 95 initiation, inhibition by Verrucarin A, 147 by membrane-bound polysomes, 125-127 posttranslational modifications, 149-151 role of endoplasmic reticulum, 117-155 by rough endoplasmic reticulum, 125-137,

148-154 in thyroid, 244, 245

Proteolysis of NADH dehydrogenase, 286 Proton translocation, in Micrococcus

lysodeikticus F1-A TPase, 352 Protoplasts, labeling by [12SIJperoxidase, 366 Pyrophosphate, effect on guaiacol peroxidase

sedimentation, 233

Qp RNA, initiation complex with 70 S ribosomes, 96

Radius of gyration of rRNA, 86 Rat liver

Index

peroxisomal fatty acyl-CoA oxidation, 181 phosphatidyl exchange proteins, 198 ribosomal turnover, 54

r-Chromatin and active transcription units, 20 from extrachromosomal rRNA genes, 18

rONA his tones, 23 nonhistone proteins, 23 non transcribed segments, 21 nucleosome chain compaction, 23 oocyte, 13 Physarum polycephalum, 21 primary transcript, 25 somatic, 13 Tetrahymena pyriformis, 11 transcription units, 25

heterogeneity, 27 Recombination, and nontranscribed

sequences, 15 Regenerating liver, peroxisomes, 185 Respiratory chain, in Micrococcus

lysodeikticus, 334 membrane potential gradient, 334

Reticulocytes, membrane protein synthesis, 133

Rhodopseudomonas sphaeroides chromatophores, 361 spheroplast antibody absorption, 312

Ribonuclease effect on rRNA, 101 from thyroid, 217

Ribonucleoprotein domains cross-linking studies, 11 in ribosomal subunits, 86-90 S4, S8, SIS, and S7 proteins, 12

Ribophorins lactoperoxidase iodination, 139 and 60 S ribosomal subunit, 139

Ribosomal genes, for eukaryotic ribosomes, 2-16

Ribosomal L-proteins, recycling, 44 Ribosomal protein L24, binding site on

rRNA,84 Ribosomal protein S4, binding site on rRNA,

84 Ribosomal proteins

asymmetry, 10

Index

Ribosomal proteins (cant) cross-linking by polyaldehydes, 11 effect of initiation factor IF-3, 99 effect on RNA-RNA interactions, 14 effect on rRNA conformation, high

temperature interactions, 15 localization in ribosomal subparticles, 81 macromolecular structure, 81 and RNA tertiary structure, 91-94 role in r RN A tertiary structure, 14 spatial organization in ribosomes, 104 in "80 S" preribosomes, 43 topography, 10

Ribosomal RNA, see rRNA Ribosomal S proteins, recycling, 44 Ribosomal subunits

reconstitution, 13 ribonucleoprotein domains, 86-90 50 S particle, 13

Ribosomes binding to membranes

effect of EDTA, 137 role of integral membrane proteins, 139

biogenesis major stages, 45 model of gene expression, 59 and nucleolar structure and function,

60 review literature, I

detachment from rough endoplasmic reticulum, 125

effect of colicin E3, 95 from E. coli, 81-104

ribosomal RNA secondary structure, 83-85

function review literature, 86-90 role of ribosomal RNA, 94-99

initiation complex with Q~ RNA, 96 intranuclear degradation. 55 from liver, effect of partial hepatectomy,

126 maturation, 42 migration, 57 mobility in rough endoplasmic reticulum,

140 protein pool, 52 proteins, effect of actinomycin D on

biosynthesis, 52 recognition of mRNA, 95

407

Ribosomes (cont.) reconstitution

cooperative effects, 98 reconstitution in vitro, 98

ribonucleoprotein segments ("domains"), 86

ribosomal protein organization, 81 spatial organization, immunoelectron

microscopy, 101 23 S rRNA, nucleotide sequence, 91-94 structural proteins, 52 structure, review literature, 82 subunits, "domains," 86 topography of rRNA, 94-99 turnover, 54 X-ray scattering studies, 100 on yeast mitochondrial surface, 195

Ribulose biphosphate carboxylase, transport of small subunit, 196

Ricin agglutinin, 363 Ricinus communis, triglyceride store, 184 RNA polymerase, adenylation, 50

effect of exotoxins, 50 in eukaryotes, 16 multiple forms, 234 in nuclei

from Chinese hamster kidney cells, 236 nucleolar turnover, 49

phosphorylation, 50 in thyroid

bimodal localization, 238 subcellular distribution, 234-238

RNA polymerase A, 16 diploid cell content, 48 effect on rRNA gene transcription, 51 metabolic stability, 49 and rRNA gene transcription, 48

RNA polymerase B, 16 RNA polymerase C, 16 RNA-protein interactions, 87 RNA-RNA interactions, 87

in ribosomal domains, 87 in terminal fraction of 23 S rRNA, 88

RNP fragments, in 30 S ribosomal subunits, 87

RNP particles, shadow casting, 103 Rough endoplasmic reticulum

continuity with smooth, 123 functional heterogeneity, 148-154 guaiacol peroxidase, 233

408

Rough endoplasmic reticulum (cont.) heterogeneity, 151 integral membrane proteins, 139 protein synthesis, 148-154 proximity to microbodies, 173 relative amount of smooth reticulum, 121 ribosome detachment, 125

effect of EDTA, 137 ribosome mobility, 148 segregation of mRNA, 149 synthesis of specific proteins

compartmentalization, 151-154 sites of synthesis, 151-154

thyroid, effect of heparin, 225 vectorial discharge of proteins, 143

rRNA conformation, 13, 15,82 effect of ionic strength, 82 effect of ribonuclease, 101 from E. coli, secondary structure, 83-85 flexibility, 15 in free and bound state, 84 gel electrophoresis, 13 genes

in Acheta domesticus, 19 active, 20 amplification

in amphibia, 5 in insects, 5

clustering, 3 differential replication, 16 in Drosophila melanogaster, 8 in Dytiscus marginalis, 19 in eukaryotes, 2-12 extrachromosomal, 5 factors affecting

elongation, 47 initiation, 47 termination, 47

introns,8 mechanism of activation, 24 in micronucleus of Tetrahymena

pyriformis, 6 nontranscribed segments, 10 number, 46 in plasmids, 30 prokaryotic, 3 promoter signals, 13 rate of transcription, 51 and RNA polymerase A, 48

rRNA (cont.) in Saccharomyces carlsbergensis, 8 in Saccharomyces cerevisiae, 8 switching on and off, 47 terminator signals, 13 transcription, 16-31,45

complex, 16-18 process, 18-29 units, 6

in Triturus, 19 in Xenopus laevis, 9, 19

hypochromic effects, 84 intranuclear wastage, 55 laser light scattering, 85 melting curve, 84 packing in subunits

neutron scattering studies, 99 X-ray studies, 99

radius of gyration, 86 in ribosomal subunits, 85-86 role in ribosome function, 94-99 secondary structure

in free state, 83-85 in ribosomes, 83-85

studies with antibodies, 103 terminal nucleotide evolution, 40 tertiary structure, 91-94

and ribosomal proteins, 14 topography in ribosomes, 94-99 translational diffusion constant, 85 tRNA binding to A site, 16 volume in ribosomal subunits, 86

rRNA pools, and pre-rRNA, 39

Index

Saccharomyces, primary pre-rRNA, 18 Saccharomyces carlsbergensis, rRNA genes,

8 Saccharomyces cerevisiae, rRNA genes, 8 Salmonella typhimurium

F,-ATPase subunit composition, 349 Iipopolysaccharides, 358

SDS-polyacrylamide gel electrophoresis of complex I, 272 and crossed immunoeiectrophoresis, 354

Secretory proteins intracellular storage, 118 role of glycosylation, 128 synthesis on membrane-bound polysomes,

127, 128 vectorial transfer, 117

Index

Serine dehydratase, synthesis on membranebound polysomes, 128

Shadow casting, RNP particles, 103 Sialic acid, in thyroid plasma membranes,

219 Sialyltransferase, in thyroid subcellular

fractions 221, 243 Signal hypothesis, 144 Signal peptides, 144 Smooth endoplasmic reticulum

in adrenal gland cells, 119 continuity with rough endoplasmic

reticulum, 123 proximity to microbodies, 173 ratio to rough endoplasmic reticulum, 121 in testis interstitial cells, 119

Sonication, thyroid microsomal fraction, 229

Soybean agglutinin, 363 Spheroplasts, from Rhodopseudomonas

sphaeroides, 312 Spherosomes

Jipases, 184 proximity to glyoxysomes, 184

"55 S" preribosomes, and "80 S" preribosome, 42

"80 S" preribosome nonribosomal proteins, 44 precursor of "55 S" preribosome, 42 protein complement, 43

21 S pre-rRNA, 38 32 S pre-rRNA, 38 36 S pre-rRNA, 38 5 S rONA, injection into Xenopus laevis

oocytes,31 30 S ribosomal subunit, digestion with

RNase, 87 50 S ribosomal subunit, proteins involved in

packing, 13 60 S ribosomal subunit

association with ribophorins, 139 interaction with membranes, 137-143 in myeloma tissue culture, 146

70 S ribosomes, chloroplastal, 196 ribulose biphosphate carboxylase synthesis,

196 S-rRNA

evolution, 32 genes, 2 intermediate pre-rRNA, 37

5 S rRNA in Drosophila melanogaster, 14 genes

in eukaryotes, 12-14 in lower eukaryotes, 12

in vitro synthesis, 31 5.8 S rRNA

genes, 2 7 S precursor, 37 terminal nucleotides, 41

16 S rRNA binding sites for IF-3, 98 N", N"-dimethyladenosine, 103 protein binding sites, 84 secondary structure, 85 3'-terminal segment and mRNA

recognition, 95 23 S rRNA, E. coli

nucleotide sequence, 83 500-nucleotide terminal fragment, 88 protein binding sites, 84

Stalked bodies in Bacillus stearothermophilus, 337 on mitochondrial inner membrane, 336

Staphylococci, surface profiles, 312 Staphylococcus aureus, cardiolipin

biosynthesis, 330

409

Steady state kinetics, NADH dehydrogenase, 270

Steroid hormone biosynthesis, in smooth endoplasmic reticulum, 119

Streptococci effect of phage muramidase, 313 surface profiles, 312

Streptococcus faecalis, membrane ATPase, 336

role of nectin, 354 Subcellular biochemistry, of thyroid, 213-251 Succinate dehydrogenase, removal of lipids, 332 Succinylated lipomannan

immunoelectrophoresis, 346 in mesosomes, 356

Supranucleosomal globules, 23

Teichuronic acid, biosynthesis in Micrococcus lysodeikticus, 324

Terminal fragment, 23 S rRNA, 88 Terminal nucleotides, in rRNA

evolution, 40 of 5.8 S rRNA, 41

410

Termination signals in primary pre-rRNA, 29 in rRNA genes, 13

Tetrahymena pyriformis r-chromatin, 18 rDNA,11 rRNA gene in micronucleus, 6 5 S rRNA genes, 12

Tetraiodothyronine (T4), formation, 214 Thyroglobulin

biosynthesis, 244 lysosomal hydrolysis, 214 mRNA,245 subunit exchange, 244

Thyroid A and B granules, 150 acid phenylphosphatase

in "mitochondrial" pellet, 242 subcellular distribution, 224

acid phospholipase, 231 adenylate cyclase, in plasma membrane

preparations, 241 alkaline phospholipase, 231 antiluminal membrane, 213 catalase, subcellular distribution, 225 cell fractionation studies, 213-231 cholesterol, in endoplasmic reticulum,

225 CMP-N-acetylneuraminic acid: GM3-

sialytransferase, subcellular distribution, 244

colloid, 213 cytochrome oxidase latency, 217 cytosolic lactate dehydrogenase, 221 deoxyribonuclease, 217 differential pelleting, 218-221 di-Na-phenylphosphatase, 217 endogenous nuclear DNA, 236 endoplasmic reticulum, cholesterol content,

225 enzyme localization, 231-238 follicles, 213 galactosyl transferase, subcellular

distribution, 221, 243 glucose-6-phosphatase, correction in assay

by phenylphosphatase, 229 ,8-glucuronidase latency, 217 ,8-glycerophosphatase, 217 Golgi apparatus, separation from plasma

membranes, 243

Thyroid (cont.) gradient centrifugation, 221-227 guaiacol peroxidase, 233 homogenization, 213-216

gel filtration of homogenates, 218 by microcavitation, 248 by Polytron homogenizer, 248 problems, 214

Index

lipolytic enzymes, subcellular localization, 231-232

liposomes, 241, 242 Long-Acting Thyroid Stimulator (LATS)

Inhibitor, 247 Iysophospholipase, 231 Iysosomes, 241, 242

acid ribonuclease activity, 228 contamination with mitochondria, 218 enzyme markers, 228 heterogeneity, 224 hydrolases, 217 phosphodiesterase activity, 228

mannosyltransferase, subcellular distribution, 221

marker enzymes, 216-218 membranes, damage by homogenization,

214 microsomal fraction, effect of sonication,

229 mitochondria

cardiolipin content, 227 contamination with Iysosomes, 218

mitochondrial/lysosomal fraction, 222 neutral phospholipase A2, 232 N-acetylglucosaminyltransferase,

subcellular distribution, 243 N-acetylhexosaminidase, in

"mitochondrial" pellet, 242 nitrogen cavitation, 248 nuclei,238-241

glucose-6-phosphatase, 229 lipids, 246 methods of isolation, 216 monolayers, 241 NADPH-cytochrome c reductase, 229 peroxidase, 229 RNA polymerase, 236

organelles, 238-251 peroxidase, subcellular distribution, 232-

234 peroxisomes, catalase activity, 225

Index

Thyroid (cant.) phenyl phosphatase, and glucose-6-

phosphatase, 229 phosphodiesterase, 217 phospholipase A, Ca2+ stimulation, 231 phospholipase A" and lysosomal markers,

232 phospholipases, 231 plasma membranes, 245-251

adenylate cyclase, 219, 249 alkaline phosphatase, 222 ATPase, 222 cholesterol, 219, 247 contamination, 246 heterogeneity, 250 lysosomal contamination, 250 method of isolation, 245 mitochondrial contamination, 250 (Na+, K+)ATPase, 249 5'-nucleotidase, 185,249 phospholipid content, 247 separation from Golgi apparatus, 243 sialic acid, 219, 247

polyribosomes, 244, 245 and thyroglobulin synthesis, 245

protein synthesis, 244, 245 ribonuclease, 217 RNA polymerase

extraction from nuclei, 236 forms lA, I., IlIA, and III., 234 possible bimodal localization, 238 subcellular localization, 234-238

rough endoplasmic reticulum, effect of heparin, 225

sialyltransferase, subcellular distribution, 221,243

subcellular biochemistry, 213-251 subcellular fractionation, technical

problems, 251 subcellular localization of

lipolytic enzymes, 231, 232 peroxidase, 232-234 RNA polymerase, 234-238

thyroglobulin biosynthesis, 244 TSH-sensitive adenylate cyclase, 249 zonal centrifugation, 222

Tibric acid, effect on peroxisomes, 180

Toyocamycin, effect on pre-mRNA biosynthesis, 53

Transcription, of rRNA genes, 16-31 in vitro studies, 29-31 transcription complex, 16-18

Transcriptional control, of ribosome biogenesis, 46-51

Transcription products, 45 S nucleolar, 30 Transcription units

definition, 6 and r-chromatin, 20 rDNA heterogeneity, 27 for rRNA genes, 2 varia tion in length, 27

"Transcripton," 6 Transglycosylation, bacterial cell-wall

biosynthesis, 323

411

Translational diffusion constant, rRNA, 85 Transpeptidation, in bacterial cell-wall

biosynthesis, 323 Triglycerides, in Ricinus communis, 184 Triiodothyronine (TJ), formation, 214 Triton X-lOO, solubilization of M.

/ysodeikticus membranes, 355 Triturus, rRNA genes, 19 Triturus a/pestris, extrachromosomal rRNA

genes, 5 tRNA

binding to A site of rRN A, 16 T,yCG sequence, 16

TSH-sensitive adenylate cyclase, 249 Turnover of ribosomes, 54 Tyrosine aminotransferase, synthesis by

membrane-bound polysomes, 128

Ubiquinol-cytochrome c oxidoreductase, 300

UDP-muramylpentapeptide, 324 UDP-N-acetyl-D-glucosamine, in

peptidoglycan biosynthesis, 323 Uricase biosynthesis, 202 Uridine, pre-rRNA conversion to

pseudouridine,32

Vectorial discharge of rough endoplasmic reticulum proteins,

143 of secretory proteins, 117

Verrucarin A effect on polysome spirals, 141 initiation inhibition, 147

412

Vesicular stomatitis virus (VSV) glycoprotein G, 192 membrane biogenesis, 191 viral envelope, 132

Vesiculation, and peroxisome biogenesis, 189

Wy-14643, effect on peroxisomes, 180

Xenopus laevis anucleolate mutants, 9 oocytes

injection of cloned 5 S rONA, 31 oocyte 5 S rONA, 13

Xenopus laevis (cont.) r-chromatin, 18 rRNA genes, 19 somatic 5 S rONA, 13

X-ray scattering of ribosomes, 100

Yeast mitochondrial F,-ATPase, 280 mitochondrial surface ribosomes,

195

Index

Zonal centrifugation, thyroid mitochondrial/ lysosomal fraction, 222

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