Heat‐shock proteins as molecular chaperones

European Journal of Biochemistry

Volumn 219, Issue 1-2, 1994, Pages 11-23

  BECKER, Jörg ^a   CRAIG, Elizabeth A ^a  

^a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN;

PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; REVIEW;

ANIMAL; ESCHERICHIA COLI; HEAT-SHOCK PROTEINS; HUMAN; MAMMALS; MULTIGENE FAMILY; PLANTS; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; SACCHAROMYCES CEREVISIAE; TRANSLATION, GENETIC;

EID: 0027954495     PISSN: 00142956     EISSN: 14321033     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1994.tb19910.x     Document Type: Article

References (191)

1. The human heat‐shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
2. Hsp70 proteins, similar to Escherichia coli DnaK, in chloroplasts and mitochondria of Euglena gracilis
3. Principles that govern the folding of protein chains
4. MAS5, a yeast homologue of DnaJ involved in mitochondrial import
5. Biogenesis of mitochondria
6. Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor
7. Eucaryotic M, 83000 heat shock protein has a homologue in Escherichia coli
8. Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
9. Identification, characterization, and DNA sequence of a functional “double” groES‐like chaperonin from chloroplasts of higher plants
10. Mechanisms of heat‐shock gene activation in higher eucaryotes
11. Interspecific nucleotide sequence comparisons used to identify regulatory and structural features of the Drosophila hsp82 gene
12. A homologue of the bacterial heat‐shock gene DnaJ that alters protein sorting in yeast
13. Transient association of newly synthesized unfolded proteins with the heat‐shock GroEL protein
14. Positive cooperativity in the functioning of molecular chaperone GroEL
15. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas
16. Molecular evolution of the HSP70 multigene family
17. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat‐shock proteins
18. hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperature
19. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase
20. Evidence that the 90‐kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
21. Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic Hsc70
22. The constitutive and stress inducible forms of hsp70 exhibit functional similarities and interact with one another in an ATP‐dependent fashion
23. GroE facilitates refolding of citrate synthase by suppressing aggregation
24. Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
25. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
26. Purification and properties of the groES morphogenetic protein of Escherichia coli
27. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins
28. The ATPase core of a clathrin uncoating protein
29. Human homologues of the bacterial heat‐shock protein DnaJ are preferentially expressed in neurons
30. Mitochondrial heat‐shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
31. Peptide sequences that target proteins for enhanced degradation during serum withdrawal
32. A role for a 70‐kilodalton heat shock protein in lysosomal degradation of intracellular proteins
33. Regulated import and degradation of a cytosolic protein in the yeast vacuole
34. 70 K heat shock related proteins stimulate protein translocation into microsomes
35. Assembly of influenza haemagglutanin trimers and its role in intracellular transport
36. The heat‐shock response
37. Is hsp70 the cellular thermometer
38. Mutations of the heat‐inducible 70 kilodalton genes of yeast confer temperature‐sensitive growth
39. Mutations in cognate gene of Saccharomyces cerevisiae HSP70 result in reduced growth rates at low temperatures
40. SSC1, a member of the 70‐kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth
41. SSC1, an essential member of the S. cerevisiae HSP70 multigene family, encodes a mitochondrial protein
42. The 90‐kDa heat shock protein (hsp‐90) possesses an ATP binding site and autophosphorylating activity
43. ATP induces a conformational change of the 90‐kDa heat shock protein (hsp90)
44. Regulation of Hsp70 function by a eukaryotic DnaJ homologue
45. Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro
46. In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90
47. Localization of the 90‐kDa heat shock protein‐binding site within the hormone‐binding domain of the glucocorticoid receptor by peptide competition
48. 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
49. Uncoating Protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis
50. A subfamily of stress proteins faciliates translocation of secretory and mitochondrial precursor polypeptides
51. Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane‐bound multisubunit complex
52. A selective pathway for degradation of cytosolic proteins by lysosomes
53. The nuclear membrane
54. Molecular chaperones
55. The molecular chaperone concept
56. Molecular cloning of mtp70, a mitochondrial member of the hsp70 family
57. Complete sequence of the heat‐inducible HSP90 gene of Saccharomyces cerevisiae
58. The groES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
59. Three dimensional structure of the ATPase fragment of a 70 K heatshock cognate protein
60. Similarity of the three‐dimensional structures of actin and the ATPase fragment of a 70‐kDa heat shock cognate protein
61. Hypothesis: Which came first, MHC class I or class II
62. Peptide binding and release by proteins implicated as catalysts of protein assembly
63. Peptide‐binding specificity of the molecular chaperone BiP
64. Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits
65. A dual role of mitochondrial hsp70 in membrane translocation of preproteins
66. Physical interaction between heat‐shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32
67. A cytoplasmic chaperonin that catalyzes β‐actin folding
68. Two cofactors and cytoplasmic chaperonin are required for the folding of α‐ and β‐tubulin
69. 1 are processed in two steps
70. Host participation in bacteriophage lambda head assembly
71. The Escherichia coli groE chaperonins
72. Expression of wild‐type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport
73. Protein folding in the cell
74. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop‐transfer mechanism
75. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MG‐ATP
76. Cooperativity in ATP hydrolysis by GroEL is increased by GroES
77. Sequence and structural homology between a mouse t‐complex protein TCP‐1 and the ‘chaperonin’ family of bacterial (groEL, 60–65 kDa heat shock antigen) and eukaryotic proteins
78. Immunoglobulin heavy chain binding protein
79. Loss of mitochondrial hsp60 function: nonequivalent effects on matrixtargeted and intermembrane‐targeted proteins
80. The signal recognition particle in S. cerevisiae
81. Protein sorting to mitochondria: evolutionary conservations of folding and assembly
82. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
83. Purification and properties of GroE, a host protein involved in bacteriophage assembly
84. Reconstitution of a heat shock effect in vitro: influence of GroE on the aggregation of α‐glucosidase from yeast
85. Activity of the Hsp70 chaperone complex DnaK, DnaJ, and GrpE in initiating phage 1 DNA replication by sequestering and releasing 1P protein
86. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly
87. Mapping the HSP90 binding region of the glucocorticoid receptor
88. Aggregated dnaA protein is dissociated and activated for DNA replication by phospholipase or dnaK protein
89. Antibodies against 70‐kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins
90. Hsp70 in the mitochondrial matrix is required for translocation and folding of precursor proteins
91. Heavy‐chain binding protein recognizes aberrant polypeptides translocated in vitro
92. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
93. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose‐regulated proteins
94. Escherichia coli SecB protein associates with exported protein precursors in vivo
95. Characterization of the Escherichia coli protein‐export gene secB
96. Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress
97. Heat shock resistance conferred by expression of the human hsp27 gene in rodent cells
98. The chaperonin GroEL binds a polypeptide in an alpha‐helical conformation
99. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
100. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone‐mediated protein folding
101. Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
102. Three pure chaperone proteins of Escherichia coli– SecB, trigger factor and GroE – form soluble complexes with precursor proteins in vitro
103. Highly conserved glucose‐regulated protein in hamster and chicken cells: preliminary characterization of its cDNA clone
104. A member of the hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK
105. TCP1 is a subunit of a heteromeric particle in the eukaryotic cytosol
106. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
107. The Escherichia coli DnaK chaperone, the 70‐kDa heat‐shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
108. The heat‐shock response
109. The heat‐shock proteins
110. (MgATP)‐dependent self‐assembly of molecular chaperone GroEL
111. Identification of a groES‐like chaperonin in mitochondria that facilitates protein folding
112. Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins
113. The structure of HLA‐B27 reveals nonamer self‐peptides bound in an extended conformation
114. The three‐dimensional structure of HLA‐B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
115. Sequential action of mitochondrial chaperones in protein import into the matrix
116. Chaperonin‐mediated protein folding at the surface of groEL through a ‘molten globule’‐like intermediate
117. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90‐kDa heat‐shock protein (hsp90) and the 94‐kDa glucose regulated protein (GRP94)
118. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
119. Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures
120. Cells in stress: transcriptional activation of heat‐shock genes
121. A TCP1‐related molecular chaperone from plants refolds phytochrome to its photoreversible form
122. An hsp70‐like protein in the ER: Identity with the 78kd glucose‐regulated protein and immunoglobulin heavy chain binding protein
123. A C‐terminal signal prevents secretion of luminal ER proteins
124. 70‐kD heat‐shockrelated protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria
125. Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane
126. Hsp90 chaperonins possess ATPase activity and bind heat‐shock transcription factors and peptidyl prolyl isomerases
127. The translation machinery and 70 kd heatshock protein cooperate in protein synthesis
128. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
129. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
130. Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix
131. Speculations on the functions of the major heat shock and glucose‐regulated proteins
132. Prechaperonin 60 and preornithine transcarbamylase share components of the import apparatus but have distinct maturation pathways in rat liver mitochondria
133. The mitochondrial protein import apparatus
134. Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria
135. Heat shock proteins Dnak and GroEL facilitate export of LacZ hybrid proteins in E. coli
136. Reduced levels of hsp90 compromise steroid receptor action in vivo
137. Dual roles of the 90‐kDa heat‐shock protein hsp90 in modulating functional activities of the dioxin receptor
138. A model of glucocorticoid receptor unfolding and stabilization by a heat‐shock protein complex
139. High molecular weight pea leaf protein similar to the groE protein of Escherichia coli
140. A human homologue of the Escherichia coli dnaJ heat shock protein
141. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
142. Involvement of a nonhormone‐binding 90‐kilodalton protein in the nontransformed 8S form of the rabbit uterus progesterone receptor
143. A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA
144. KAR2, a karyogamy gene, is the yeast homologue of the mammalian BiP/GRP78 gene
145. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum
146. Enzymatic recycling of clathrin from coated vesicles
147. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells
148. A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to dnaJ, an Escherichia coli heat shock protein
149. The molybdate‐stabilized glucocorticoid binding complex of L‐cells contains a 98–100 Kdalton nonsteroid‐binding phosphoprotein that is part of the murine heat‐shock complex
150. Relationship of the 90‐kDa murine heat‐shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor
151. HSP104 required for induced thermotolerance
152. Hsp104 is required for tolerance to many forms of stress
153. Genetic evidence for a functional relationship between hsp104 and hsp70
154. Sec61p and BiP directly facilitate polypeptide translocation into the ER
155. A precursor protein partially translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein
156. An enzyme that removes clathrin coats: purification of an uncoating ATPase
157. Enzymatic dissociation of clathrin cages in a two‐stage process
158. Mitochondrial precursor protein. Effects of 70‐kilodalton heat shock protein on polypeptide folding, aggregation, and import competence
159. The transport of proteins into the nucleus requires the 70‐kilodalton heat shock protein or its cytosolic cognate
160. A major testicular cell protein specified by a mouse T/t complex gene
161. The E. coli dnak gene product, the hsp70 homologue, can reactivate heatinactivated RNA polymerase in an ATP hydrolysis‐dependent manner
162. The glucose‐regulated protein grp94 is related to heat‐shock protein hsp90
163. Self regulation of 70 kilodalton heat shock proteins in Saccharomyces cerevisiae
164. The heat‐shock response of E. coli is regulated by changes in the concentration of sigma‐32
165. The activity of sigma‐32 is reduced under conditions of excess heat‐shock protein production in E. coli
166. DnaK, DnaJ, and GrpE heat‐shock proteins negatively regulate heat‐shock gene expression by controlling the synthesis and stability of sigma 32
167. Purification and characterization of the chaperonin 10 and chaperonin 60 proteins from Rhodobacter sphaeroides
168. Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73‐kDa heat‐shock cognate protein
169. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t‐complex polypeptide‐1
170. The 70 KD mammalian heat‐shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelions from coated vesicles
171. A Drosophila melanogaster gene encodes a protein homologous to the mouse t complex polypeptide 1
172. The yeast homolog to Mouse Tcp‐1 affects microtubule‐mediated processes
173. Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60
174. Complex interaction between the chaperonin 60 molecular chaperone and dihydrofolate reductase
175. Loss of BiP/grp78 function blocks translocation of secretory proteins in yeast
176. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on hsp70 in the matrix
177. Mechanisms of translocation across the ER membrane
178. Nuclear and nucleolar localization of the 72,000–dalton heat‐shock protein in heat‐shocked mammalian cells
179. Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
180. Yeast Hsp70 RNA levels change in response to the physiological status of the cell
181. Monomerization of RepA dimers by heat‐shock proteins activates binding to DNA replication origin
182. DnaJ, DnaK, and GrpE heat‐shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step
183. Hsp90 chaperones protein folding in vitro
184. DnaK and DnaJ heat‐shock proteins participate in protein export in Escherichia coli
185. The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat‐shock protein
186. Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1
187. TCP1 complex is a molecular chaperone in tubulin biogenesis
188. Zuotin, a putative Z‐DNA binding protein in S. cerevisiae
189. The yeast SIS1 protein, a dnaJ homologue, is required for the initiation of translation
190. Seventy‐kilodalton heat‐shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes