Elsevier S & T

Protein Folding in the Cell

Horwich, Arthur

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Table of contents

Title Pageiii
Copyright Pageiv
CONTENTSv
PREFACExi
Chapter 1. Hsp70 Chaperone Machines1
I. Introduction1
II. Chaperone Activities of Hsp702
III. Mechanism of Action8
IV. The Targeting Activity of Co-chaperones28
V. Outlook36
References37
Chapter 2 .Allostery and Protein Substrate Conformational Change during GroEL/GroES-Mediated Protein45
I. Introduction45
II. Structure of GroEL and Its Functional Complexes46
III. Polypeptide Folding56
IV. Conclusions70
References71
Chapter 3. Type II Chaperonins, Prefoldin, and the Tubulin-Specific Chaperones73
I. Introduction73
II. Discovery of Type II Chaperonins and Early Functional Studies74
III. Subunits and Assembly75
IV. Target Range and Specificity of CCT79
V. Cycling of Target Proteins by CCT81
VI. Genetics83
VII. Structure of Type II Chaperonins84
VIII. Prefoldin88
IX. Tubulin-Specific Chaperones92
X. Conclusion98
References98
Chapter 4. Structure and Function of the Small Heat Shock Protein/α-Crystallin Family of Molecular105
I. Introduction105
II. Diversity of the sHsps and Their Expression Patterns107
III. X-Ray Structural Analysis116
IV. Dynamic Nature of the sHsp Oligomer124
V. sHsp Chaperone Activity127
VI. Potential sHsp Substrates138
VII. Conclusions146
References147
Chapter 5. Structure, Function, and Mechanism of the Hsp90 Molecular Chaperone157
I. Introduction157
II. Domain Structure and Function158
III. ATP Binding and Hydrolysis by Hsp90 Are Essential in Vivo164
IV. Conformational Changes in Hsp90 Accompanying the ATPase Cycle166
V. Hsp90 ATPase Inhibitors„A New Class of Antitumor Drugs170
VI. Interaction with Co-chaperones173
VII. Regulation of ATP Binding and Hydrolysis in the Client-Protein Activation Pathway175
VIII. Interactions with Alterations of Client Proteins by Hsp90176
IX. Conclusion180
References181
Chapter 6. The Proteasome: A Supramolecular Assembly Designed for Controlled Proteolysis187
I. Introduction187
II. The 20S Proteasome188
III. Activators of the 20S Proteasome202
IV. Conclusions213
References213
Chapter 7. Hsp70 Proteins in Protein Translocation223
I. Introduction223
II. Protein Translocation into Mitochondria and ER224
III. Cytosolic Hsp70s Are Involved in Protein Translocation227
IV. Hsp70 and Its Cofactors228
V. Lumenal Hsp70s and Protein Translocation229
VI. Other Roles for Hsp70s in Protein Translocation237
VII. Conclusion238
References239
Chapter 8. Prolyl Isomerases243
I. Perspective244
II. Properties of Prolyl Peptide Bonds244
III. Prolyl Isomerizations in Protein Folding246
IV. Examples250
V. Cis/trans Isomerizations at Nonprolyl Peptide Bonds253
VI. Prolyl Isomerizations in Folded Proteins255
VII. Prolyl Isomerases256
VIII. Prolyl Isomerases as Catalysts of in Vitro Protein Folding261
IX. The Trigger Factor264
X. Catalysis of Prolyl Isomerization during de Novo Protein Folding267
XI. Cellular Functions of Prolyl Isomerases268
XII. Concluding Remarks273
References274
Chapter 9. Catalysis of Disulfide Bond Formation and Isomerization in Escherichia coli283
I. Introduction283
II. De Novo Formation of Disulfide Bonds in E. coli: The Discovery of DsbA284
III. DsbA Is the Most Oxidizing Disulfide Catalyst286
IV. DsbB Provides the Periplasm with Oxidizing Power290
V. Correcting Wrong Disulfide Bonds in the Periplasm: Disulfide Bond Isomerization by DsbC292
VI. DsbD Provides Reducing Equivalents in a Highly Oxidizing Environment296
VII. Dsb Proteins and Cytochrome c Maturation297
VIII. Disulfide Bond Formation Does Not Interfere with Disulfide Isomerization298
IX. Concluding Remarks298
References299
Chapter 10. N-Glycan Processing and Glycoprotein Folding303
I. Introduction303
II. N-Glycan Processing in the Endoplasmic Reticulum304
III. Glycoprotein Reglucosylation308
IV. Chaperones and Protein Folding in the Endoplasmic Reticulum320
V. Interaction of Glycoproteins with Calnexin and Calreticulin321
VI. Calnexin and Calreticulin Are Lectins Specific for Monoglucosylated Oligosaccharides323
VII. N-Glycan Processing and Glycoprotein Degradation330
VIII. Summary and Future Perspectives332
References333
Chapter 11. Functional Genomic Approaches to Understanding Molecular Chaperones and Stress Responses345
I. Introduction345
II. Historical Perspective346
III. Functional and Genomic Analysis of the Unfolded Protein Response353
VI. UPR as a Case Study in the Comparison of Supervised versus Unsupervised Searches376
References380
Chapter 12. The Yeast Prion [PSI+]: Molecular Insights and Functional Consequences391
I. Overview391
II. Reversible Curing395
III. Separating Prion Initiation and Propagation400
IV. Conformational Replication in Vitro402
V. Functional Consequences of the [PSI +] State406
VI. Conclusion409
References409
Chapter 13. Clp ATPases and Their Role in Protein Unfolding and Degradation413
I. Introduction413
II. Clp ATPase Family of Proteins414
III. Chaperone Activity of Clp ATPases and Their Participation in Proteolysis415
IV. Structure of Clp ATPases: Alone and with Partner Proteases416
V. Mechanism of Action of Clp ATPases as Chaperones and as Components of Degradation Machinery419
VI. Clp ATPase Specificity Factors425
VII. Summary426
References426
AUTHOR INDEX431
SUBJECT INDEX481
Color Plate SectionColor Plate-1

Book details

Vendor Elsevier S & T
SKU 9780120342594
ISBN-13 9780080522401
Author Horwich, Arthur
Category Medical
Subject Biochemistry

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This volume of Advances in Protein Chemistry provides a broad, yet deep look at the cellular components that assist protein folding in the cell. This area of research is relatively new--10 years ago these components were barely recognized, so this book is a particularly timely compilation of current information. Topics covered include a review of the structure and mechanism of the major chaperone components, prion formation in yeast, and the use of microarrays in studying stress response. Outlines preceding each chapter allow the reader to quickly access the subjects of greatest interest. The information presented in this book should appeal to biochemists, cell biologists, and structural biologists.

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