Molecular chaperones in the cell:
Saved in:
| Format: | Book |
|---|---|
| Language: | English |
| Published: |
Oxford [u.a.]
Oxford Univ. Press
2001
|
| Edition: | 1. Publ. |
| Series: | Frontiers in molecular biology
37 |
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XX, 281 S. Ill., graph. Darst. |
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| adam_text | Contents
List of contributors xvii
Abbreviations xix
1 Cellular functions of cytosolic E. coli chaperones 1
AXEL MOGK, BERND BUKAU, AND ELKE DEUERLING
1. Introduction 1
2. Major cytosolic E. coli chaperones 3
2.1 The HsplOO/Clp chaperones 3
2.2 The HtpG (Hsp90) chaperone 4
2.3 The DnaK (Hsp70) chaperone system 5
2.4 The GroEL (Hsp60) chaperone system 7
2.5 The IbpA/IbpB (small Hsps) chaperones 8
2.6 Trigger factor (TF) 9
3. Housekeeping activities of cytosolic E. coli chaperones 10
3.1 De novo folding of proteins in the E. coli cytosol 10
3.1.1 Co translational folding of nascent polypeptides at the ribosome 10
3.1.2 Post translational folding in the cytosol 14
3.2 Protein quality control in the E. coli cytosol 16
3.3 Involvement of cytosolic E. coli chaperones in protein secretion 17
3.4 Protection of thermolabile E. coli proteins during heat stress 18
3.5 Protection of E. coli proteins during oxidative stress 21
4. Specialised functions of cytosolic E. coli chaperones: protein activity
control by the DnaK system 22
5. Summary and perspectives 23
Acknowledgements 24
References 24
2 Chaperones in secretion pathways of E. coli 35
NELLIE HARMS, JOEN LUIRINK, BAUKE OUDEGA
1. General introduction 35
NTENTS
2. Cytoplasmic chaperones and secreted proteins 35
2.1 Introduction 35
2.2 Trigger factor 36
2.3 Signal recognition particle 37
2.3.1 Structural aspects 37
2.3.2 Recognition by SRP: who and where 39
2.3.3 The targeting pathway 40
2.4 General chaperones, the heat shock proteins 41
2.5 Secretion dedicated chaperone, SecB 42
2.5.1 Structural aspects 42
2.5.2 Preprotein recognition 42
2.5.3 Interaction with SecA 43
3. Membrane chaperones 44
4. Periplasmic chaperones and secreted proteins 44
4.1 Introduction 44
4.2 LPS and phospholipids 46
4.3 Skp 46
4.4 Disulfide oxidoreductases (Dsbs) 47
4.5 Peptidyl prolyl cis/trans isomerases (PPIases) 49
4.6 LolA 49
4.7 The PapD chaperone family 49
5. Summary and conclusions 51
References 52
3 The role of chaperone proteins in the import and
assembly of proteins in mitochondria and chloroplasts 61
WOLFGANG VOOS AND NIKOLAUS PFANNER
1. Introduction 61
2. Mitochondrial biogenesis 62
2.1 Protein membrane translocation 62
2.1.1 Preproteins: targeting signals and import competence 62
2.1.2 Translocase complexes in outer and inner membrane 64
2.1.3 Membrane potential (AY) 65
2.2 Function of mtHsp70 in driving membrane translocation 65
2.2.1 Tim44 as membrane anchor 66
2.2.2 Driving force for polypeptide translocation 66
2.2.3 Mgelp as nucleotide exchange factor for mtHsp70 67
CONTENTS xi
2.3 Preprotein folding in the mitochondrial matrix 69
2.3.1 mtHsp70: coupling between translocation and folding process 69
2.3.2 Mdjlp/Mdj2p:co chaperonesofmtHsp70 69
2.3.3 Other mitochondrial Hsp70s 70
2.3.4 Hsp60 / HsplO:high molecular weight folding machinery 70
2.4 Protein complex assembly and degradative processes 71
2.4.1 Hsp78 / Mcxlp: homologues of bacterial Clp family of chaperones 72
2.4.2 Chaperone functions involved in protein assembly and degradation 73
3. Chloroplast biogenesis 73
3.1 Translocation across the envelope membranes 73
3.1.1 Targeting signals and import competence 74
3.1.2 Docking and outer envelope translocation 75
3.1.3 Inner envelope translocation 76
3.2 Chaperones involved in chloroplast transport and folding 76
3.2.1 Com70 at the outer surface 76
3.2.2 Hsp70 IAP in the intermembrane space 77
3.2.3 HsplOO/ClpCinthestroma 77
3.2.4 StromalHsp70 77
3.2.5 Chaperonin 60 system 78
4. Comparison of chloroplast and mitochondrial membrane
translocation 79
Acknowledgements 80
References 81
4 The roles of the cytosolic chaperone, CCT, in normal
eukaryotic cell growth 90
KEITH R. WILLISON AND JULIE GRANTHAM
1. Introduction 90
2. The CCT complex 91
2.1 Composition of CCT 91
2.2 Structure of CCT 93
2.3 Substrates of CCT in vitro and in vivo 97
2.4 Regulation of CCT expression 99
2.5 Analysis of CCT in yeast 101
2.6 Mechanism of action 104
2.7 GIM/prefoldin 104
2.8 Tubulin cofactors 106
2.9 Evolution of CCT and the eukaryotic cytoskeleton 108
xii ¦ CONTENTS
3. Conclusions m
Acknowledgements 112
References ^^
5 The roles of the major cytoplasmic chaperones in
normal eukaryotic cell growth: Hsc70 and its cofactors 119
CHRISTINE PFUND, WEI YAN, AND ELIZABETH CRAIG
1. Chaperones involved in protein biogenesis 119
1.1 Hsp / Hsc70 functions in protein synthesis 120
1.1.1 Interaction of Hsp/Hsc70 of mammalian cells with nascent polypeptides 121
1.1.2 Ribosome associated Hsp70s of Saccharomyces cerevisiae 122
1.1.3 Hsp70s and initiation of translation 124
1.2 Hsp40s involved in nascent chain synthesis and folding 124
1.2.1 Hdj 1 and Hdj 2 of mammalian cells 125
1.2.2 Hsp40s in S, cerevisiae 127
1.3 Chaperone machines involved in protein biogenesis 128
2. Chaperones in post translational translocation of proteins into
organelles 131
2.1 Protein import into the endoplasmic reticulum 131
2.2 Protein import into mitochondria 132
2.3 Protein import into peroxisomes 133
2.4 Protein import into the lysosome 133
2.5 Protein import into the nucleus 134
3. Chaperones involved in the disassembly of protein complexes:
uncoating of clathrin 134
4. Summary 136
References 137
6 Hsp70 chaperone networks: the role of regulatory
co chaperones in co ordinating stress responses with
cell growth and death 142
JAEWHAN SONG AND RICHARD I. MORIMOTO
1. Introduction 142
2. The Hsp70 family of molecular chaperones and co chaperones 143
3. The family of Hsp70 proteins 145 {
3.1 Hsp70 family 145 j
3.2 HspllO family 145 1
3.3 Biochemical and biophysical features of Hsp70 146 I
CONTENTS | xiii
4. DnaJ 147
4.1 General features of the DnaJ family 147
4.2 DnaJ homologs of E. coli, S. cerevisiae, and humans 147
4.3 Mitochondrial DnaJ proteins 151
4.4 DnaJ endoplasmic reticulum homologues 151
4.5. Other DnaJ homologues 152
5. Bagl 152
6. Hip and Hop (p60) 153
7. Conclusion 153
Acknowledgements 154
References 154
7 Chaperones in signal transduction 164
DAVID F. SMITH
1. Hsp90 and signalling proteins 164
2. Hsp90, Hsp70, and their partners 164
3. Target specific chaperone preferences 167
4. Functional significance 168
4.1 Signalling proteins compared to model misfolded substrates for
chaperone interactions 168
4.2 Stabilization and folding of signalling proteins by chaperones 169
4.2.1 Steroid receptors 169
4.2.2 Src family tyrosine kinases 170
4.3 Functional repression of signalling proteins by chaperones 171
4.4 Functional modulation of signalling proteins by chaperones 173
5. Concluding comments 174
Acknowledgements 174
References 174
8 Molecular chaperone systems in the endoplasmic
reticulum 180
MARC F. PELLETIER, JOHN J. M. BERGERON, AND DAVID Y. THOMAS
1. Introduction 180
2. The calnexin cycle 181
2.1 Discovery of calnexin, and its characterization as an ER lectin like
chaperone 181
CONTENTS
2.2 The lectin/true molecular chaperone debate 183
2.3 The calnexin/Erp57 folding complex 185
2.4 Quality control of protein folding for N linked glycoproteins in the ER 186
2.4.1 The role of de/reglucosylation in quality control and protein folding 187
3. Retrotranslocation of proteins from the ER 188
3.1 ER associated degradation and genetic disease 188
3.2 Where does ER associated degradation occur, in the ER or cytosol? 189
3.3 ERAD of membrane and soluble ER proteins 190
3.3.1 The proteasome degrades ER membrane proteins 191
3.3.2 Soluble lumenal proteins are also degraded by a cytosolic degradation
pathway 191
3.4 Membrane and soluble secretory proteins must cross the ER membrane
barrier, but how? 191
3.5 Some possible mechanisms for retrotranslocation through the Sec61
translocon channel 192
3.6 Proteins with unknown function 193
3.7 The mannosidase clock: a model for the selective process associated
with ERAD 193
4. Signalling from the ER 194
4.1 The unfolded protein response in yeast 195
4.2 The mammalian UPR 196
4.3 Irelp and PERK in the regulation of other cellular responses to ER stress 198
5. Concluding remarks 199
Acknowledgements 199
References 200
9 The function of chaperones and proteases in protein
quality control and intracellular protein degradation 205
MICHAEL MAURIZI
1. General introduction 205
2. Intracellular protein degradation 206
2.1 Proteolysis as part of protein quality control 206
2.2 Recognition of appropriate substrates for degradation 208
2.3 Motifs used to target proteins for degradation 209
2.4 A bipartite binding model for protein degradation 211
3. The major ATP dependent proteolytic systems 212
3.1 Structural features of ClpAP and ClpXP 212
3.2 Functional domains of ClpA and ClpX 214
CONTENTS xv
3.3 Comparison of structures of ClpAP and the proteasome 215
3.4 Lon and FtsH, multiple functional domains in a single polypeptide 216
4. Enzymatic properties of ATP dependent proteases 216
4.1 Protein and peptide degradation activities 216
4.2 Chaperone activities of ClpA and ClpX 216
4.3 Chaperone activities of ATP dependent protease holoenzyme
complexes 217
4.4 The reaction pathway for ATP dependent protein degradation 218
4.5 Kinetic partitioning of substrates between release and translocation 220
5. The action and interaction of chaperones and proteases in vivo 220
5.1 Cooperation between chaperones and proteases 221
5.2 Is autonomous chaperone and protease interaction direct or indirect? 222
5.3 Independent chaperone activity of components of ATP dependent
proteases 222
5.4 Homologues of ATP dependent proteases with autonomous chaperone
activity 223
5.5 Regulation by proteases: applying the coup de grace 224
6. Challenges for the future 225
References 226
10 Regulation of expression of molecular chaperones 235
PETER LUND
1. Introduction 235
2. Chaperone gene expression in prokaryotes 235
2.1 Expression of many cytoplasmic chaperones is constitutive and is
up regulated by heat shock and related stresses 235
2.2 The presence of unfolded protein is a signal for elevation of chaperone
expression in the cytoplasm 237
2.3 In E. coli, heat shock inducible molecular chaperones are regulated by
the t32 factor of RNA polymerase 238
2.4 In E. coli, a32 levels are regulated in part by unfolded protein via the
DnaK/DnaJ chaperones 240
2.5 tr32 levels are also modulated directly by temperature 241
2.6 The E. coli system is unusual: most bacteria appear to use repressor
based mechanisms to regulate the major cytoplasmic chaperones 243
2.7 Levels of the HrcA repressor are controlled by the GroE chaperone
system 245
2.8 Extra cytoplasmic unfolded proteins in £. coli also induce a chaperone
response 246
xvi CONTENTS
3. Chaperone gene expression in eukaryotes 246
3.1 Stress induced cytoplasmic chaperones are activated by the heat shock
transcription factor (HSF) 248
3.2 Unfolded proteins can induce a heat shock response in eukaryotes 249
3.3 Molecular chaperones modulate HSF activity 249
4. Summary of major points 250
References 251
11 Partial unfolding as a precursor to amyloidosis:
a discussion of the occurrence, role, and implications 257
NEIL M. KAD AND SHEENA E. RADFORD
1. Introduction 257
1.1 Amyloid fibril structure 258
1.2 Amyloid fibril precursors 263
2. Transthyretin 265
2.1 Inhibition studies 268
3. Light chain amyloid 268
4. P2 microglobulin 269
5. Discussion 272
Acknowledgements 273
References 273
Index 279
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| indexdate | 2024-07-09T18:52:27Z |
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| physical | XX, 281 S. Ill., graph. Darst. |
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| series | Frontiers in molecular biology |
| series2 | Frontiers in molecular biology |
| spelling | Molecular chaperones in the cell ed. by Peter Lund 1. Publ. Oxford [u.a.] Oxford Univ. Press 2001 XX, 281 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Frontiers in molecular biology 37 Cytochemie gtt Moleculaire chaperonnes gtt Molécules chaperonnes Molecular Chaperones Molecular chaperones Chaperonine (DE-588)4338035-9 gnd rswk-swf Hitzeschock-Proteine (DE-588)4255487-1 gnd rswk-swf Polypeptidketten bindende Proteine (DE-588)4311255-9 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Polypeptidketten bindende Proteine (DE-588)4311255-9 s DE-604 Hitzeschock-Proteine (DE-588)4255487-1 s Chaperonine (DE-588)4338035-9 s Lund, Peter Sonstige oth Frontiers in molecular biology 37 (DE-604)BV010329078 37 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009445449&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Molecular chaperones in the cell Frontiers in molecular biology Cytochemie gtt Moleculaire chaperonnes gtt Molécules chaperonnes Molecular Chaperones Molecular chaperones Chaperonine (DE-588)4338035-9 gnd Hitzeschock-Proteine (DE-588)4255487-1 gnd Polypeptidketten bindende Proteine (DE-588)4311255-9 gnd |
| subject_GND | (DE-588)4338035-9 (DE-588)4255487-1 (DE-588)4311255-9 (DE-588)4143413-4 |
| title | Molecular chaperones in the cell |
| title_auth | Molecular chaperones in the cell |
| title_exact_search | Molecular chaperones in the cell |
| title_full | Molecular chaperones in the cell ed. by Peter Lund |
| title_fullStr | Molecular chaperones in the cell ed. by Peter Lund |
| title_full_unstemmed | Molecular chaperones in the cell ed. by Peter Lund |
| title_short | Molecular chaperones in the cell |
| title_sort | molecular chaperones in the cell |
| topic | Cytochemie gtt Moleculaire chaperonnes gtt Molécules chaperonnes Molecular Chaperones Molecular chaperones Chaperonine (DE-588)4338035-9 gnd Hitzeschock-Proteine (DE-588)4255487-1 gnd Polypeptidketten bindende Proteine (DE-588)4311255-9 gnd |
| topic_facet | Cytochemie Moleculaire chaperonnes Molécules chaperonnes Molecular Chaperones Molecular chaperones Chaperonine Hitzeschock-Proteine Polypeptidketten bindende Proteine Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009445449&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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