Anthony L. Fink - Molecular chaperones in the life cycle of proteins: structure, function, and mode of action
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Molecular chaperones in the life cycle of proteins: structure, function, and mode of action
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Considers the integral role of molecular chaperones at different stages of a proteins life cycle. The text focuses on the biophysical, structural and functional properties of molecular chaperones, providing a biophysical view of chaperone problems useful in in vivo and in vitro studies, and augmenting current understanding of molecular chaperones as facilitators of de novo protein synthesis and recombinant protein folding.
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Molecular Chaperones in the Life Cycle of Proteins : Structure, Function, and Mode of Action
author
:
Fink, Anthony L.
publisher
:
CRC Press
isbn10 | asin
:
0824701003
print isbn13
:
9780824701000
ebook isbn13
:
9780585157689
language
:
English
subject
Molecular chaperones--Physiological effect.
publication date
:
1998
lcc
:
QP552.M64M65 1998eb
ddc
:
572/.645
subject
:
Molecular chaperones--Physiological effect.
Page i
Molecular Chaperones in the Life Cycle of Proteins
Structure, Function, and Mode of Action
Edited by Anthony L. Fink University of California, Santa Cruz Santa Cruz, California Yuji Goto Osaka University Osaka, Japan
MARCEL DEKKER, INC. NEW YORK BASEL HONG KONG
Page ii
Fink, Anthony L. Molecular chaperones in the life cycle of proteins: structure, function, and mode of action/Anthony L. Fink, Yuji Goto p. cm. Includes index. ISBN 0-8247-0100-3 (hardcover) 1. Molecular chaperonesPhysiological effect. I. Goto, Yuji. II. Title. QP552.M64F56 1997 572'.645dc21
97-34429 CIP
The publisher offers discounts on this book when ordered in bulk quantities. For more information, write to Special Sales/Professional Marketing at the address below.
This book is printed on acid-free paper.
Copyright 1998 by MARCEL DEKKER, INC. All Rights Reserved.
Neither this book nor any part may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, microfilming, and recording, or by any information storage and retrieval system, without permission in writing from the publisher.
MARCEL DEKKER, INC. 270 Madison Avenue, New York, New York 10016 http://www.dekker.com
Proteins come and go; in the cell, their lifetimes and steady-state concentrations are determined by the relative rates of protein synthesis and degradation. The life of a protein may be considered to be the sum of events and processes beginning with its synthesis on the ribosome and ending (normally) with its final degradation by proteases into its constituent amino acids. Throughout its lifetime, but especially at the beginning and end, the protein is assisted by chaperones, various other proteins that facilitate the desired course of events for the target protein. These molecular chaperones may be highly specific in that they interact with only one target protein, or a very limited number of target proteins. One such example is PapD, which is involved in the assembly of pili. They also may be very promiscuous and interact with most of the proteins in a cell, such as Hsp60 and Hsp70, which play an important role in the folding of nascent polypeptide chains. In this book, we have taken the unusual approach of considering the molecular chaperones from the perspective of their role in guiding proteins through their life cycle, from the cradle to the grave.
The heat shock protein and molecular chaperone field is an extremely active one. It encompasses studies ranging from basic biophysical properties of the chaperone proteins themselves, through their enzyme-like functions and reaction cycles, their genetic regulation, their key role in combating stress at the cellular level, and their role in a wide variety of diseases. In the context of the life cycle of proteins, the emphasis of this book is on the former three areas. The major classes of general chaperones (as opposed to dedicated or specific chaperones) are Hsp100, Hsp90, Hsp70, Hsp60, Hsp40, and the small heat shock proteins. Recent investigations have shown that not only do the major classes of chaper-
Page iv
ones often function with protein cofactors, but interactions between members of the Hsp40, Hsp60, Hsp70, and Hsp90 families may be frequent.
The basic paradigm of molecular chaperones is that they bind unfolded, or relatively unfolded, polypeptides (but not native or native-like conformations) to form relatively stable complexes. In some cases, these are dissociated by the binding and hydrolysis of adenosine triphosphate (ATP). The more well-defined constitutive roles of heat shock proteins are facilitating (chaperoning) the folding and assembly of newly synthesized polypeptides, and facilitating the translocation of proteins across membranes, such as those of the mitochondria. The induced roles of heat shock proteins involve their ability to help the cell cope with stress, and are not emphasized in this volume. Although we now know a great deal about the major chaperone families, as indicated in this treatise, we know much less about the many cofactors that are also suspected of being involved. Although many chaperones are heat shock proteins or stress proteins, many are not, and are implicated only in various aspects of the normal functioning of the cell.
Although a few monographs have been published on molecular chaperones, these have emphasized their role as stress proteins, rather than facilitators of protein folding and degradation. Sufficient recent progress has been made in our understanding of the role of the molecular chaperones in various aspects of protein synthesis and degradation, and the biophysical, structural, and functional properties of the chaperones themselves, to justify the present volume. Putting this material in the context of the life cycle of proteins provides an interesting and unique perspective. A detailed understanding of how proteins fold to their native structures, both in vitro and in vivo, and how they are degraded, remain major challenges of cellular and molecular biology. In one sense this volume is a status report on recent progress in these areas.
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