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The biology of heat shock proteins and molecular chaperones
J-lBS 19 - DECEMBER
BOOKREVIEWS
1994
total nine chapters dealing with various forms of electrophoresis, plus several others detailing methods for detecting materials within gels. The use of blotting for the identification of proteins and their posttranslationally modified products is now an everyday molecular technique, and there are several excellent chapters describing blotting and detection systems that can be used for protein characterization with immunological and lectin-based reagents. The inclusion of chemiluminescent and gold or immunogold detection methods links well with chapters on the use of protein A and avldin-biotin. 1turned to the four chapters towards the end of the book that dealt with antibody production, and found these to be full of useful technical information. The chapter on the production of monoclonal antibodies was extremely lucid, and the reassurance of the author of the benefits of persistence in hybridoma production struck a chord of realism for me! Further chapters detail how antibodies can be used for detection and analytical procedures. In total this volume shows the prospective researcher how to put together a range of related techniques, all of which are described clearly with helpful support commentary. The quality
of a multi-author volume can often be determined by the care taken over referencing and cross-referencing between chapters. Thus, it would seem selfdefeating that, in a volume describing the Lowry and other protein quantitation assays in detail (Chapters l-3). the author of Chapter 14 should refer the reader to another publication. Yet there is evidence that significant attention has been put into the references. When 1 came across the use of PAGE blue 83 (a name 1 had not encountered before, and which was not defined in the chapter) in Chapter 5,1 checked the index to find that it was cross-referenced to Coomassie brilliant blue R250. So what do 1 think of this book? Are there aspects that I feel are missing, and how does it compete in a field with so many other methodological and techniques books? The predecessor of this volume was the first of the Methods in Molecular Biology series, and this current volume offers a well-updated review of basic techniques. Although most of the techniques can be found in other publications, they are produced here as a single linked package and explained at a readily understandable level. Additionally, the ‘Notes’ sections inspire in the reader (at least this reader) the feeling that the authors were writing from real hands-on technical knowledge.
If there is an aspect that could be expanded it is towards the examination of post-translational protein modification. For example, aspects related to the analysis of protein phosphorylation would have integrated well with the technologies described here for glycosylation and peptide mapping. This is a competitive area for publications; would I buy this volume? I think that the answer to this is yes. It is a useful and concise volume that would be of great value around the lab. I would also recommend it for libraries as it provides an excellent reference source on techniques of protein analysis for undergraduates entering the difficult world of research projects. The value of this volume lies in the fact that any potential reader is liable to use the techniques described in several chapters to pursue a piece of research work. The editor indicates that there are plans to produce a companion volume that would cover preparative techniques used for proteins. I look forward to the appearance of this volume; together the two will be a useful source of reference.
Putting stress on chaperones
extremely fast moving and, despite the rapid progress made, a precise understanding of the function of molecular chaperones is still lacking. There is, however, a general consensus that a common denominator for the function of HSPs - and some non-HSPs is the modulation of protein folding and unfolding events in the cell. The term ‘molecular chaperone’ has provided a unifying and descriptive concept in this respect. The predecessor of this monograph Stress Proteins in Biology and Medicine’, also edited by ‘the three musketeers’, Morimoto, Tissieres and Georgopoulos, has set the standards high. It served well as a reference book summarizing the state of the art in the heat-shock field around 1990. In the present monograph, 86 authors have been recruited to write about 22 different heat-shock- and chaperone-related topics, ihcluding protein translocation, protein folding, thermotolerance, DNA replication, protein export and involvement of HSPs in disease. The editors succeed in compiling a multifaceted, up-to-date view of the biology of HSPs. The introductory chapter, written by the editors, gives an excellent integrated view of the field,
thus putting the rather diverse articles of the book into a general perspective. It provides novices to the field with an account of the status quo, and also with an idea for the open questions and the directions the field is going. In general, the authors of the individual chapters naturally give a personal but, in most cases, balanced and comprehensive overview of particular aspects of HSP function, regulation of the heat-shock response and involvement of HSPs in disease. Thus, this book deserves to attract a large audience which, by nature of the topics covered, will be rather diverse in interest. Although not all the models presented may stand the test of time, the book is an invaluable source of information for anybody interested in HSPs.
TheBiologyof HeatShockProteins andMolecularChaperones edited by R. 1. Morimoto, A. Tissihs and C. Georgopoulos, Cold Spring Harbor laboratory Press, 1994. $97.00 (vii + 610 pages) /SBN 0 87969 427 0 The study of heat shock or stress proteins @ISPs) has evolved as one of the most fascinating areas of biomedical research over the past decade. Besides having a protective function under unphysiological stress conditions, HSPs seem to be involved in many fundamental aspects, ranging from transcriptional regulation to autoimmunity, from protein translocation to receptor-mediated endocytosis and proteolysis. Given this functional heterogeneity and the fact that HSPs fall into a number of different structural and functional subclasses, compiling a balanced and upto-date monograph on this topic is a rather dangerous and daring enterprise, especially because the heat shock field is
ALAN J. DICKSON School of Biological Manchester, Oxford Ml3 9PT.
Sciences, University of Road, Manchester, UK
Reference 1 Morimoto, R. I., TissiBres, A. and Georgopoulos, C. (1990) Stress Proteins Biology and Medicine, Cold Spring Harbor Laboratory Press
JOHANNES
in
BUCHNER
Institute of Biophysics and Physical Biochemistry, Universitit Regensburg, D-93040 Regensburg. Germany.
559
BOOKREVIEWS
1994
total nine chapters dealing with various forms of electrophoresis, plus several others detailing methods for detecting materials within gels. The use of blotting for the identification of proteins and their posttranslationally modified products is now an everyday molecular technique, and there are several excellent chapters describing blotting and detection systems that can be used for protein characterization with immunological and lectin-based reagents. The inclusion of chemiluminescent and gold or immunogold detection methods links well with chapters on the use of protein A and avldin-biotin. 1turned to the four chapters towards the end of the book that dealt with antibody production, and found these to be full of useful technical information. The chapter on the production of monoclonal antibodies was extremely lucid, and the reassurance of the author of the benefits of persistence in hybridoma production struck a chord of realism for me! Further chapters detail how antibodies can be used for detection and analytical procedures. In total this volume shows the prospective researcher how to put together a range of related techniques, all of which are described clearly with helpful support commentary. The quality
of a multi-author volume can often be determined by the care taken over referencing and cross-referencing between chapters. Thus, it would seem selfdefeating that, in a volume describing the Lowry and other protein quantitation assays in detail (Chapters l-3). the author of Chapter 14 should refer the reader to another publication. Yet there is evidence that significant attention has been put into the references. When 1 came across the use of PAGE blue 83 (a name 1 had not encountered before, and which was not defined in the chapter) in Chapter 5,1 checked the index to find that it was cross-referenced to Coomassie brilliant blue R250. So what do 1 think of this book? Are there aspects that I feel are missing, and how does it compete in a field with so many other methodological and techniques books? The predecessor of this volume was the first of the Methods in Molecular Biology series, and this current volume offers a well-updated review of basic techniques. Although most of the techniques can be found in other publications, they are produced here as a single linked package and explained at a readily understandable level. Additionally, the ‘Notes’ sections inspire in the reader (at least this reader) the feeling that the authors were writing from real hands-on technical knowledge.
If there is an aspect that could be expanded it is towards the examination of post-translational protein modification. For example, aspects related to the analysis of protein phosphorylation would have integrated well with the technologies described here for glycosylation and peptide mapping. This is a competitive area for publications; would I buy this volume? I think that the answer to this is yes. It is a useful and concise volume that would be of great value around the lab. I would also recommend it for libraries as it provides an excellent reference source on techniques of protein analysis for undergraduates entering the difficult world of research projects. The value of this volume lies in the fact that any potential reader is liable to use the techniques described in several chapters to pursue a piece of research work. The editor indicates that there are plans to produce a companion volume that would cover preparative techniques used for proteins. I look forward to the appearance of this volume; together the two will be a useful source of reference.
Putting stress on chaperones
extremely fast moving and, despite the rapid progress made, a precise understanding of the function of molecular chaperones is still lacking. There is, however, a general consensus that a common denominator for the function of HSPs - and some non-HSPs is the modulation of protein folding and unfolding events in the cell. The term ‘molecular chaperone’ has provided a unifying and descriptive concept in this respect. The predecessor of this monograph Stress Proteins in Biology and Medicine’, also edited by ‘the three musketeers’, Morimoto, Tissieres and Georgopoulos, has set the standards high. It served well as a reference book summarizing the state of the art in the heat-shock field around 1990. In the present monograph, 86 authors have been recruited to write about 22 different heat-shock- and chaperone-related topics, ihcluding protein translocation, protein folding, thermotolerance, DNA replication, protein export and involvement of HSPs in disease. The editors succeed in compiling a multifaceted, up-to-date view of the biology of HSPs. The introductory chapter, written by the editors, gives an excellent integrated view of the field,
thus putting the rather diverse articles of the book into a general perspective. It provides novices to the field with an account of the status quo, and also with an idea for the open questions and the directions the field is going. In general, the authors of the individual chapters naturally give a personal but, in most cases, balanced and comprehensive overview of particular aspects of HSP function, regulation of the heat-shock response and involvement of HSPs in disease. Thus, this book deserves to attract a large audience which, by nature of the topics covered, will be rather diverse in interest. Although not all the models presented may stand the test of time, the book is an invaluable source of information for anybody interested in HSPs.
TheBiologyof HeatShockProteins andMolecularChaperones edited by R. 1. Morimoto, A. Tissihs and C. Georgopoulos, Cold Spring Harbor laboratory Press, 1994. $97.00 (vii + 610 pages) /SBN 0 87969 427 0 The study of heat shock or stress proteins @ISPs) has evolved as one of the most fascinating areas of biomedical research over the past decade. Besides having a protective function under unphysiological stress conditions, HSPs seem to be involved in many fundamental aspects, ranging from transcriptional regulation to autoimmunity, from protein translocation to receptor-mediated endocytosis and proteolysis. Given this functional heterogeneity and the fact that HSPs fall into a number of different structural and functional subclasses, compiling a balanced and upto-date monograph on this topic is a rather dangerous and daring enterprise, especially because the heat shock field is
ALAN J. DICKSON School of Biological Manchester, Oxford Ml3 9PT.
Sciences, University of Road, Manchester, UK
Reference 1 Morimoto, R. I., TissiBres, A. and Georgopoulos, C. (1990) Stress Proteins Biology and Medicine, Cold Spring Harbor Laboratory Press
JOHANNES
in
BUCHNER
Institute of Biophysics and Physical Biochemistry, Universitit Regensburg, D-93040 Regensburg. Germany.
559