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Chaperones / edited by Marja Makarow, Ineke Braakman. — Berlin ; New York : Springer, c2006.—(58.17421/C462) |
Contents
Contents
Regulation of the heat shock response by heat shock transcription factors 1
Ville Hietakangas and Lea Sistonen 1
Abstract 1
1 Preface 1
2 Transcriptional regulation of the heat shock response in bacteria 2
3 Regulation of the eukaryotic heat shock response via heat shock elements 3
4 Heat shock factors constitute a conserved family of transcriptional regulators 4
5 HSF 1 -the prototypical heat shock transcription factor 7
6 HSF2 - a cooperative modulator of HSFI? 15
7 HSF3 - an avian-specific regulator of heat shock genes 17
8 HSF4 - regulator of eye development 18
9 Novel functions for HSFs in transcription 18
10 Conclusions and perspectives 22
Acknowledgements 23
References 23
The unfolded protein response unfolds 35
Maho Niwa 35
Abstract 35
1 Endoplasmic reticulum (ER): the journey to secretion 35
2 The unfolded protein response (UPR) pathway 37
3 Mammalian UPR 40
4 Phospholipids and the UPR 47
5 UPR signaling arm specific components identified to date 48
6 BiP associates with the luminal domains of IRE1， PERK， and ATF6 50
7 Time dependent shift of the UPR response 51
8 Physiological roles of the UPR 52
9 Conclusions 53
Acknowledgements 54
References 54
Hspl04p: a protein disaggregase 65
Johnny M. Tkach and John R. Glover 65
Abstract 65
1 Hspl04p and thermotolerance in yeast 65
2 In vitro reconstitution of Hsp104p refolding activity 68
3 Hsp100 structure and function 70
4 Mechanism of protein disaggregation 73
5 Organization of the bichaperone network 76
6 Yeast prions and Hspl04p 77
7 Implications for protein aggregation disease 82
8 Final Remarks 84
References 84
Folding of newly synthesised proteins in the endoplasmic reticulum 91
Sanjika Dias-Gunasekara and Adam M. Benham 91
Abstract 91
1 The scope of protein folding in the ER 91
2 Entry into the ER 92
3 ER protein sorting 93
4 Signal peptide cleavage 93
5 The proline problem 95
6 Folding of ER glycoproteins 96
7 BiP 100
8 Disulfide bond formation 100
9 Introducing more ER chaperones 104
10 Folding of specialised proteins in the ER 104
11 Techniques， model systems and what's next 106
Acknowledgements 107
References 107
Abbreviations 116
Quality control of proteins in the mitochondrion 119
Mark Nolden， Brigitte Kisters-Woike， Thomas Langer， and Martin Graef 119
Abstract 119
1 Stability of mitochondria 119
2 Molecular chaperone proteins and mitochondrial proteolysis 121
3 ATP-dependent proteases of mitochondria 122
4 Quality control of inner membrane proteins 131
5 Regulation of quality control systems of mitochondria 136
References 137
Chaperone proteins and peroxisomal protein import 149
Wim de Jonge， Henk F. Tabak， and Ineke Braakman 149
Abstract 149
1 Introduction 149
2 Peroxisomes 150
3 Involvement of Hsp70 in peroxisomal protein import 162
4 Involvement of Hsp90 in peroxisomal protein import 170
5 Concluding remarks 172
References 173
Proteasomal degradation of misfolded proteins 185
Robert Gauss， Oliver Neuber， and Thomas Sommer 185
Abstract 185
1 Introduction .... 185
2 Recognition and degradation of aberrant proteins in the cytosol 186
3 Protein degradation from the ER 195
4 Cdc48p/p97 chaperoning poly-ubiquitinated proteins 204
5 Diseases and toxins - what can go wrong in protein degradation? 206
6 Conclusions 211
Acknowledgement 211
References 212
Template-induced protein misfolding underlying prion diseases 221
Luc Bousset， Nicolas Fay， and Ronald Melki 221
Abstract 221
1 Prion diseases 221
2 Formulation of the prion hypothesis 222
3 The mammalian prion PrP 222
4 The prions in yeast and fungi 224
5 Properties of the fibrillar forms of prion proteins 229
6 Soluble oligomeric forms of the prion proteins 231
7 Mechanistic models for prion propagation 231
8 Maintenance and inheritance 232
9 In vitro assembly process of prions proteins 234
10 Prions and misfolding diseases， unquestioned issues， and unanswered questions 237
11 Conclusions and perspectives 239
References 239
The Hsp60 chaperonins from prokaryotes and eukaryotes 251
M. Giulia Bigotti， Anthony R. Clarke， and Steven G. Burston 251
Abstract 251
1 The Group I chaperonins 251
2 Structure of the Group I chaperonins 254
3 Interaction between Group I chaperonins and protein substrate 257
4 Allostery and asymmetry in nucleotide binding to GroEL 257
5 Reaction cycle of the Group I chaperonins 259
6 The Group I chaperonin-assisted protein folding reaction 263
7 The Group II chaperonins 264
8 Group II chaperonin subunit composition and organization 266
9 Structure of the Group II chaperonins 267
10 Nucleotide-induced structural rearrangements in the Group II chaperonins 269
11 Allostery in the Group II chaperonins 271
12 Interaction between the Group II chaperonins and protein substrates 273
13 Future perspectives 274
References 275
Index 285
