The action of molecular chaperones in the early secretory pathway

Annual Review of Genetics

Volumn 35, Issue , 2001, Pages 149-191

  Fewell, S W ^a   Travers, K J ^a   Weissman, J S ^a   Brodsky, J L ^a  

^a UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

Calnexin; ERAD; Hsp40; Hsp70; Oxidative protein folding; UPR

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70;

BIOGENESIS; CATALYSIS; CYTOPLASM; ENDOPLASMIC RETICULUM; ENZYME SPECIFICITY; ESCHERICHIA COLI; FUNGAL GENETICS; MOLECULAR GENETICS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECRETION; REVIEW; SACCHAROMYCES CEREVISIAE;

ANIMALS; BIOLOGICAL TRANSPORT; ENDOPLASMIC RETICULUM; HUMANS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEINS; QUALITY CONTROL;

ESCHERICHIA COLI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0035675962     PISSN: 00664197     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.genet.35.102401.090313     Document Type: Review

References (299)

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45. 70K heat shock related proteins stimulate protein translocation into microsomes
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47. The cyclophilin homolog ninaA is required in the secretory pathway
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69. The UDP-Glc: Glycosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress
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72. A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc: Glycoprotein glucosyltransferase
73. Peptide binding specificity of the molecular chaperone BiP
74. Pathways for protein disulphide bond formation
75. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
76. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
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80. Post-translational disruption of the ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes ΔF508 CFTR in the rabbit reticulocyte lysate
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83. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone
84. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin
85. Protein folding in the cell
86. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase
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88. Can hsp70 proteins act as force-generating motors?
89. Purification and properties of a microsomal enzyme system catalyzing the reactivation of reduced ribonuclease and lysozyme
90. Mechanism of nonspliceosomal mRNA splicing in the unfolded protein response pathway
91. The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes
92. Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70
93. Cer1p, a novel hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast
94. The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
95. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocation pore before and early in translocation
96. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
97. Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
98. Quality control in the secretory pathway
99. Role of the 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
100. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
101. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation
102. The signal recognition particle in yeast
103. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
104. Evolutionary conservation of components of the protein translocation complex
105. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
106. Accumulating evidence suggests AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
107. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
108. The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
109. Intracellular functions of N-linked glycans
110. Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system
111. 1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ (1-78)
112. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
113. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
114. Competition between folding and glycosylation in the endoplasmic reticulum
115. A pathway for targeting soluble misfolded proteins to the yeast vacuole
116. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
117. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
118. Protein oligomerization in the endoplasmic reticulum
119. Oxidized redox state of gluthathione in the endoplasmic reticulum
120. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
121. Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome
122. Retrieval of transmembrane proteins to the endoplasmic reticulum
123. Degradation of mis-folded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
124. Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent
125. In vivo reactivation of heat-denatured protein in the endoplasmic reticulum of yeast
126. The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability
127. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
128. The translocon: A dynamic gateway at the ER membrane
129. Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains
130. Hop modulates Hsp70/Hsp90 interactions in protein folding
131. An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
132. Sls1p stimulates the Sec63p-mediated activation of Kar2p in a conformation dependent manner in the yeast endoplasmic reticulum
133. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
134. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
135. Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Haclp/Em4p that activates the unfolded protein response
136. Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen
137. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
138. Derl, a novel protein specifically required for endoplasmic reticulum degradation in yeast
139. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
140. Catalysis of protein folding by prolyl isomerase
141. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated folding
142. Yeast mutants affecting possible quality control of plasma membrane proteins
143. Escherichia coli DnaJ and grpE heat shock proteins jointly stimulate ATPase activity of DnaK
144. Ratcheting in post-translation protein translocation: A mathematical model
145. Oligosaccharide modification in the early secretory pathway directs the selection of a mis-folded glycoprotein for degradation by the proteasome
146. SHR3: A novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast
147. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae
148. Quality control by proteases in the endoplasmic reticulum. Removal of a protease-sensitive site enhances expression of human P-glycoprotein
149. Re-orientation of aquaporin-1 topology during maturation in the endoplasmic reticulum
150. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
151. Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of S. cerevisiae
152. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
153. The protein conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
154. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
155. Role of the proteasome in membrane extraction of a short-lived ER transmembrane protein
156. The role of ATP in the functional cycle of the DnaK chaperone system
157. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during post-translational protein translocation into the yeast ER
158. Mutation of the ATP binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum
159. Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
160. Yeast mutants deficient in ER-associated degradation of the Z variant of alpha-1-protease inhibitor
161. Degradation of 3-hydroxymethyl-3-glutaryl-Coa reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
162. The hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
163. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
164. Mammalian Sec61 is associated with Sec62 and Sec63
165. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
166. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
167. Signalling from endoplasmic reticulum to nucleus: Transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway
168. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
169. A 22bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
170. Degradation of HMG-CoA reductase in vitro. Cleavage in the membrane domain by a membrane-bound cysteine protease
171. The peptide-binding domain of the chaperone protein hsc70 has an unusual secondary structure topology
172. Molecular mechanism of membrane protein integration into the endoplasmic reticulum
173. A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae
174. Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane
175. Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway
176. The PBN1 gene of Saccharomyces cerevisiae: An essential gene that is required for the post-translational processing of the protease B precursor
177. Mnl1p, an α-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for ER associated degradation of glycoproteins
178. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
179. The translation machinery and 70kd heat shock protein cooperate in protein synthesis
180. Dynamics and retention of misfolded proteins in native ER membranes
181. Signal sequences specify the targeting route to the endoplasmic reticulum membrane
182. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
183. Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation
184. The yeast Jem1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion
185. Molecular chaperones in the yeast ER maintain the solubility of proteins for retrotranslocation and degradation
186. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
187. Functional differences in yeast protein disulfide isomerases
188. S. cerevisiae encodes an essential protein in sequence and function to mammalian BiP
189. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
190. Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidylinositol-linked protein in a pre-Golgi compartment
191. Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae
192. Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
193. Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
194. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
195. The calnexin homologue cnx1+ in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain
196. Protein glycosylation and its role in protein folding
197. Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides
198. Folding of active β-lactamase in the yeast cytoplasm before translocation into the endoplasmic reticulum
199. NMR structure of the J-domain and the Gly-Phe-rich region of the Escherichia coli DnaJ chaperone
200. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex
201. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
202. Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum
203. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
204. Mutant analysis links the translocon and BIP to retrograde protein transport for ER degration
205. Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome
206. Retrograde protein translocation: Eradication of secretory proteins in health and disease
207. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
208. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
209. Nuclear magnetic resonance solution structure of the human hsp40 (HDJ-1) J-domain
210. Degradation of a mutant secretory protein, α1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
211. Post-translational protein translocation across the membrane of the endoplasmic reticulum
212. Molecular chaperones: Towards a characterization of the heatshock protein 70 family
213. Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum
214. The genetics of disulfide bond metabolism
215. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
216. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
217. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
218. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
219. A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein
220. Sec61p and BiP directly facilitate polypeptide translocation into the ER
221. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates
222. Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression
223. The Hsp90 family - An overview
224. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with Bip/Kar2p via a conserved domain that specifies interactions with hsp70s
225. Kinetics of molecular chaperone action
226. Cholera toxin is exported from microsome by the Sec61p complex
227. In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER
228. Pharmacologic shifting of a balance between protein protein refolding and degradation mediated by Hsp90
229. Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation
230. Splicing: Hacking into the unfolded-protein response
231. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
232. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
233. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
234. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
235. What drives the translocation of proteins?
236. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
237. Ricin A chain utilizes the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast
238. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
239. Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog
240. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
241. The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins
242. Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
243. Protein folding in the ER
244. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26S proteasome
245. Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ
246. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
247. PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase
248. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
249. The ATP hydrolysis dependent cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE
250. NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain
251. The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae
252. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
253. Endoplasmic reticulum (ER)-associated degradation of misfolded glycoprotein is suppressed upon inhibition of ER mannosidase I
254. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
255. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
256. A conserved HPD sequence of the J domain is neccessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
257. Biochemical basis of oxidative protein folding in the endoplasmic reticulum
258. Homologs of the yeast Sec complex sub-units Sec62p and Sec63p are abundant proteins in dog pancreas microsomes
259. LHS1 and SIL1 provide lumenal function that is essential for protein translocation into the endoplasmic reticulum
260. Proteasomal proteomics: Identifcation of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
261. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
262. The 26S proteasome: A molecular machine designed for controlled proteolysis
263. The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication
264. The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
265. Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
266. Eps1, a novel PDI-related protein involved in ER quality control in yeast
267. Identification of the peptide binding domain of hsc70. 18-kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding
268. Cloning of mammalian Ire1 reveals diversity in the ER stress responses
269. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
270. Degradation of CFTR by the ubiquitin proteasome pathway
271. Secretory protein translocation in a yeast cell-free system can occur post-translationally and requires ATP hydrolysis
272. Protein folding and assembly in the endoplasmic reticulum
273. Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor
274. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor
275. Proteasome-dependent ER-associated protein degradation: An unconventional route to a familiar fate
276. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol
277. Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA
278. Sec61p-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
279. Endoplasmic reticulum degradation of a subunit of the asialoglycoprotein receptor in vitro. Vesicular transport from endoplasmic reticulum is unnecessary
280. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
281. The transmembrane anchor of the T-cell antigen receptor beta chain contains a structural determinant of pre-Golgi proteolysis
282. Degradation of T-cell receptor chains in the endoplasmic reticulum is inhibited by inhibitors of cysteine proteases
283. Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation
284. Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain
285. Zuotin, a ribosome-associated DnaJ molecular chaperone
286. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
287. Identification of the cis-acting endoplasmic reticulum stress response element responsible for trancriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
288. Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo
289. Cytosolic degradation of T-cell receptor α chains by the proteasome
290. Protein folding in a specialized compartment: The endoplasmic reticulum
291. A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
292. Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
293. The Hsp70 molecular chaperone facilitates the ER associated protein degradation of the cystic fibrosis transmembrane conductance regulator in yeast
294. The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation
295. The engagement of Sec61p in the ER dislocation process
296. Structural analysis of substrate binding by the molecular chaperone DnaK
297. Protein disulfide bond synthesis: A possible intracellular mechanism
298. Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes
299. Initiation of λ DNA replication with purified host and bacteriophage encoded proteins: The role of the DnaK, DnaJ, and grpE heat shock proteins