Molecular chaperones in the cell / edited by Peter Lund.

Format:

Book

Contributor:

Lund, Peter A.

Series:

Frontiers in molecular biology ; 37.

Frontiers in molecular biology ; 37

Language:

English

Subjects (All):

Molecular chaperones.

Physical Description:

xx, 281 pages : illustrations ; 26 cm.

Place of Publication:

Oxford ; New York : Oxford University Press, 2001.

Contents:

1 Cellular functions of cytosolic E. coli chaperones / Axel Mogk, Bernd Bukau, Elke Deuerling 1

2. Major cytosolic E. coli chaperones 3

2.1 The Hsp100 / 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

2 Chaperones in secretion pathways of E. coli / Nellie Harms, Joen Luirink, Bauke Oudega 35

2. Cytoplasmic chaperones and secreted proteins 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

4.2 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

3 The role of chaperone proteins in the import and assembly of proteins in mitochondria and chloroplasts / Wolfgang Voos, Nikolaus Pfanner 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 ([Delta gamma]) 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 Mge1p as nucleotide exchange factor for mtHsp70 67

2.3 Preprotein folding in the mitochondrial matrix 69

2.3.1 mtHsp70: coupling between translocation and folding process 69

2.3.2 Mdj1p / Mdj2p: co-chaperones of mtHsp70 69

2.3.3 Other mitochondrial Hsp70s 70

2.3.4 Hsp60 / Hsp10:high molecular weight 'folding machinery' 70

2.4 Protein complex assembly and degradative processes 71

2.4.1 Hsp78 / Mcx1p: 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 Hsp100 / ClpC in the stroma 77

3.2.4 Stromal Hsp70 77

3.2.5 Chaperonin 60 system 78

4. Comparison of chloroplast and mitochondrial membrane translocation 79

4 The roles of the cytosolic chaperone, CCT, in normal eukaryotic cell growth / Keith R. Willison, Julie Grantham 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

5 The roles of the major cytoplasmic chaperones in normal eukaryotic cell growth: Hsc70 and its cofactors / Christine Pfund, Wei Yan, Elizabeth Craig 119

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

6 Hsp70 chaperone networks: the role of regulatory co-chaperones in co-ordinating stress responses with cell growth and death / Jaewhan Song, Richard I. Morimoto 142

2. The Hsp70 family of molecular chaperones and co-chaperones 143

3. The family of Hsp70 proteins 145

3.1 Hsp70 family 145

3.2 Hsp110 family 146

3.3 Biochemical and biophysical features of Hsp70 146

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. Bag1 152

6. Hip and Hop (p60) 153

7 Chaperones in signal transduction / David F. Smith 164

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

8 Molecular chaperone systems in the endoplasmic reticulum / Marc F. Pelletier, John J. M. Bergeron, David Y.

Thomas 180

2. The calnexin cycle 181

2.1 Discovery of calnexin, and its characterization as an ER lectin-like chaperone 181

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

9 The function of chaperones and proteases in protein quality control and intracellular protein degradation / Michael Maurizi 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

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

10 Regulation of expression of molecular chaperones / Peter Lund 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 [sigma superscript 32] factor of RNA polymerase 238

2.4 In E. coli, [sigma superscript 32] levels regulated in part by unfolded protein via the DnaK/DnaJ chaperones 240

2.5 [sigma superscript 32] 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 E. coli also induce a chaperone response 246

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

11 Partial unfolding as a precursor to amyloidosis: a discussion of the occurrence, role, and implications / Neil M. Kad, Sheena E. Radford 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. [beta subscript 2]-microglobulin 269.

Notes:

Includes bibliographical references and index.

ISBN:

0199638675

OCLC:

45743302