Microbial molecular chaperones

Advances in Microbial Physiology

Volumn 44, Issue , 2001, Pages 93-140

  Lund, Peter A ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

CYTOLOGY; GENE EXPRESSION REGULATION; HEAT SHOCK; MOLECULAR BIOLOGY; NONHUMAN; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN SYNTHESIS; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TRANSLATION REGULATION;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034982311     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2911(01)44012-4     Document Type: Review

References (197)

1. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
2. Principles that govern the folding of protein chains
3. The heat-shock regulated gene grpE of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds
4. Two different mechanisms are involved in the heat-shock regulation of chaperonin gene expression in Bradyrhizobium japonicum
5. Ancient heat shock gene is dispensable
6. Chaperonin-dependent increase in Cu-Zn superoxide dismutase production in Escherichia coli
7. How chaperones fold proteins
8. At sixes and sevens: Characterisation of the symmetry mismatch of the CIpAP chaperone-assisted protease
9. Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coli
10. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
11. The crystal structure of bacterial chaperonin GroEL at 2.8 angstroms
12. The dnaK operon of Streptomyces coelicolor encodes a novel heat shock protein which binds to the promoter region of the operon
13. Regulation of the dnaK operon of Streptomyces coelicolor A3(2) is governed by HspR, an autoregulatory repressor protein
14. The HspR regulon of Streptomyces coelicolor: A role for the DnaK chaperone as a transcriptional co-repressor
15. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
16. Regulation of the Escherichia coli heat shock response
17. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicates roles for heat shock protein in normal metabolism
18. ΔdnaK mutants of Escherichia coli have defects in chromosomal segregation and plasmid maintenance at normal growth temperatures
19. Mutations altering the heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
20. Purification and properties of the GroES morphogenetic protein of Escherichia coli
21. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryoelectron microscopy
22. Characterisation of twenty six new heat shock genes of Escherichia coli
23. A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a Type III topology
24. Mutations in Hsp83 and cdc37 impair signalling by the sevenless receptor tyrosine kinase in Drosophila
25. Streptomyces lividans groES, groEL1 and groEL2 genes
26. Requirement of the Escherichia coli dnaK gene for thermotolerance and protection against hydrogen peroxide
27. Trigger factor and DnaK cooperate in folding of newly synthesised proteins
28. Purification and characterization of Chromatium vinosum GroEL and GroES proteins overexpressed in Escherichia coli cells lacking the endogenous groESL operon
29. Molecular characterisation of two groEL genes in Streptomyces coelicolor A3(2)
30. Protein unfolding and the energetics of protein translocation across biological membranes
31. The general concept of molecular chaperones
32. Molecular chaperones - Opening and closing the Anfinsen cage
33. Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat-shock regulatory gene
34. In vivo observation of polypeptide flux through the bacterial chaperone system
35. Periplasmic protein thiol: Disulfide oxidoreductases of Escherichia coli
36. Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
37. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
38. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
39. One member of a groESL-like chaperonin multigene family in Bradyrhizobium japonicum is co-regulated with symbiotic nitrogen fixation genes
40. GroEL chaperonins are required for the formation of a functional nitrogenase in Bradyrhizobium japonicum
41. GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells
42. Successive action of Escherichia coli chaperones in vivo
43. The mature part of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export
44. Immunolocalization of Hsp60 in Legionella pneumophila
45. Surface-associated Hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
46. Bacterial mutants which block phage assembly
47. Host participation in bacteriophage lambda assembly
48. The complete sequence of the mucosal pathogen Ureaplasma urealyticum
49. Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
50. Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes
51. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends upon two chaperonin proteins and Mg-ATP
52. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
53. GroES binding regulates GroEL chaperonin activity under heat shock
54. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
55. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminus peptide tails added by the SsrA-tagging system
56. Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans
57. Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction
58. Co-operation of GroEL/GroES and Dnak/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
59. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
60. Function and regulation of the heat shock proteins
61. The htpR gene product of E. coli is a sigma factor for heat-shock promoters
62. 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli
63. A survey of the heat shock response in four Streptomyces species reveals two groEL-like genes and three GroEL-like proteins in Streptomyces albus
64. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
65. Homologous plant and bacterial proteins chaperone oligomeric protein assembly
66. Levels of major proteins of Escherichia coli during growth at different temperatures
67. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
68. Purification of GroE, a host protein involved in bacteriophage assembly
69. 32, the heat shock regulator in Escherichia coli, is governed by Hf1B
70. Role of the DnaK and HscA homologs of Hsp70 in protein folding in E. coli
71. Escherichia coli trigger factor is a prolyl-isomerase that associates with nascent polypeptide chains
72. Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly
73. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
74. Folding in vivo of bacterial cytoplasmic proteins - Role of GroEL
75. Identification of in vivo substrates of GroEL
76. Diverse effects of the MalE-LacZ hybrid protein in Escherichia coli cell physiology
77. Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 degrees C but not at 43 degrees C
78. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase: Implications for heat shock in vivo
79. Chaperone activity with a redox switch
80. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES
81. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes the binding of GroEL to unfolded proteins
82. Effects of reduced levels of GroE chaperones on protein metabolism - Enhanced synthesis of heat-shock proteins during steady state growth of Escherichia coli
83. 32 in Escherichia coli
84. Synergistic roles of HsIVU and other ATP-dependent proteases in controlling in vivo turnover of sigma(32) and abnormal proteins in Escherichia coli
85. Mutations in a gene encoding a new hsp70 suppress rapid DNA inversion and bgl activation but not prou derepression in hns-1 mutant Escherichia coli
86. The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat shock from Escherichia coli cells
87. Crystal structure of the signal sequence binding subunit of the signal recognition particle
88. Positive control of the two-component RcsC/B signal transduction network by DjIA: A member of the DnaJ family of molecular chaperones in Escherichia coli
89. Homology in structural organization between the E. coli CIpAP protease and the eukaryotic 26S proteasome
90. Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli
91. Substrate specificity of the SecB chaperone
92. Mycobacterium tuberculosis expresses two chaperonin-60 homologues
93. Molecular chaperones and protein translocation across the Escherichia coli inner membrane
94. Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo
95. SecB stabilizes a translocation-competent state of purified prePhoE protein
96. Heat shock protein GroE of Escherichia coli: Key protective roles against thermal stress
97. Effects of mutations in heat shock genes groES and gruEL on protein export in Escherichia coli
98. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone mediated protein folding
99. Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock: HtrA protease action in vivo and in vitro
100. IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock
101. Three pure chaperone proteins of Escherichia coli, secB, trigger factor and GroEL, form soluble complexes with precursor protein in vitro
102. ProOmpA contains secondary and tertiary structure and is shielded from aggregation by association with SecB
103. Effect of the over-production of the heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli
104. Cloning and characterisation of two groESL operons of Rhodobacter sphaeroides: Transcriptional regulation of the heat induced groESL operon
105. Hsc66, an hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock
106. Disassembly of the Mu-transposase tetramer by the CIpX chaperone
107. GroEL under heat-shock - Switching from a folding to a storing function
108. Folding with a two-stroke motor
109. An alternative protein targeting pathway in Escherichia coli: Studies on the role of FtsY
110. Functional integration of a polytopic membrane protein of E. coli requires the bacterial signal recognition particle
111. GroE is vital for cell wall synthesis
112. Role of HrcA and CIRCE in the heat shock regulatory network of Bradyrhizobium japonicum
113. Protein folding in the bacterial periplasm
114. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
115. Nonnative proteins induce expression of the Bacillus subtilis CIRCE regulon
116. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and CIpB
117. Translational induction of heat shock transcription factor sigma(32): Evidence for a built-in RNA thermosensor
118. 32 level in Escherichia coli
119. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and CIpB chaperones
120. Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers
121. Interplay of two cis-acting elements in translation control of synthesis during the heat shock response of Escherichia coli
122. Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscAhscB-hscA-fdx-ORF3 gene cluster
123. The Rhizobium meliloti groELc locus is required for regulation of early nod genes by the transcription activator NodD
124. Bacterial genes induced within the nodule during the Rhizobium-legume symbiosis
125. Escherichia coli dnaK null mutants are inviable at high temperature
126. Induction of a heat shock like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation
127. Protein disaggregation mediated by the heat shock protein Hsp104
128. Generation of a stable folding intermediate which can be rescued by the chaperonins GroES and GroEL
129. Heat-shock proteins DnaK and GruEL facilitate export of LacZ hybrid proteins in E. coli
130. Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain
131. Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins
132. Chaperonins
133. The Escherichia coli chaperonin 60 (groEL) is a potent stimulator of osteoclast formation
134. The ins and outs of a molecular chaperone machine
135. Genome-wide expression profiling in Escherichia coli K-12.1
136. The genetics of disulfide bond metabolism
137. Mycobacteria contain two groEL genes: The second Mycobacterium leprae groEL gene is arranged in an operon with groES
138. An essential role for the Escherichia coli DnaK protein in starvation induced thermotolerance, H202 resistance and reductive division
139. Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
140. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
141. Substrate specificity of the DnaK chaperone determined by screening cellulose bound peptide libraries
142. Cloning and characterisation of multiple groEL chaperonin genes in Rhizobium meliloti
143. Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12
144. Organization and expression of the dnaJ and dnaK genes of Escherichia coli K12
145. PapD-like chaperones and pilus biogenesis
146. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
147. Overproduction, purification and characterisation of GroES and GroEL from thermophilic Bacillus stearothermophilus
148. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
149. Isolation and analysis of mutants of the dnaK operon of Bacillus subtilis
150. Regulation and organization of the dnaK and groE operons in Eubacteria
151. Isolation and characterisation of dnaJ null mutants of Escherichia coli
152. Use of new Escherichia coli/Streptomyces conjugative vectors to probe the functions of the two groEL-like genes of Streptomyces albus G by gene disruption
153. The RheA repressor is the thermosensor of the HSP18 heat shock response in Streptomyces albus
154. Biochemical characterisation of the small heat shock protein IbpB from Escherichia coli
155. Chaperonin function: Folding by forced unfolding
156. Structure and function in GroEL-mediated protein folding
157. The Hsc66-Hsc20 chaperone system in Escherichia coli: Chaperone activity and interactions with the DnaK-DnaJ-GrpE system
158. Catalysis of protein folding by symmetric chaperone complexes
159. The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori
160. Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits
161. A ribosome-associated peptidylprolyl cis/trans isomerase identified as the trigger factor
162. 32
163. Escherichia coli heat shock gene mutants are defective in proteolysis
164. 32 is reduced under conditions of excess heat shock protein production in Escherichia coli
165. 32
166. Cloning, characterisation and functional analysis of groESL operon from thermophilic cyanobacterium Synechococcus vulcanus
167. Polypeptide flux through bacterial Hsp70: DnaK co-operates with trigger factor in chaperoning nascent chains
168. The chaperone/usher pathway: A major terminal branch of the general secretory pathway
169. Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: Comparison with CIpA, CIpB and HtpG in vivo
170. 32
171. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli
172. A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli
173. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
174. Nascent membrane and presecretory proteins sythesised in Escherichia coli associate with signal recognition particle and trigger factor
175. The Escherichia coli SRP and SecB targeting pathways converge at the translocon
176. Demonstration by genetic suppression of interaction of GroE products with many proteins
177. Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins
178. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
179. Participation of Escherichia coli K-12 groE gene products in the synthesis of cellular DNA and RNA
180. Rhizobium leguminosarum contains multiple chaperonin (cpn60) genes
181. Thinking outside the box: New insights into the mechanism of GroEL-mediated protein folding
182. The structure of CIpP at 2.3 angstrom resolution suggests a model for ATP-dependent proteolysis
183. A molecular chaperone, CIpA, functions like DnaK and DnaJ
184. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
185. Accumulation of secretory protein precursors in Escherichia coli induces the heat shock response
186. Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
187. Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides
188. The heat-shock protein CIpB in Escherichia coli is a protein-activated ATPase
189. The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex
190. Hsc62, a new DnaK homologue of Escherichia coli
191. Regulation of GroE expression in Bacillus subtilis: The involvement of the σA like promoter and the roles of the inverted repeat sequence (CIRCE)
192. The universally conserved GroE (Hsp60) chaperonins
193. Isolation and characterisation of Escherichia coli mutants that lack the heat-shock sigma factor sigma 32
194. Structural analysis of substrate binding by the molecular chaperone DnaK
195. Estimation of the macromolecular concentrations and excluded volume effects for the cytoplasm of Escherichia coli
196. CIpB cooperates with DnaK, DnaJ and GrpE in suppressing protein aggregation - A novel multi-chaperone system from Escherichia coli
197. CIRCE, a novel heat-shock element involved in regulation of heat-shock operon dnaK or Bacillus subtilis