Nucleotide Exchange Factor for the Yeast Hsp70 Molecular Chaperone Ssa1p

REFERENCES

• Adams, A., D. E. Gottschling, C. A. Kaiser, and T. Stearns. 1997. Methods in yeast genetics. A Cold Spring Harbor Laboratory course manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Agashe, V. R., and F. U. Hartl. 2000. Roles of molecular chaperones in cytoplasmic protein folding. Semin. Cell Dev. Biol. 11: 15–25.
   PubMed Web of Science ®Google Scholar
• Ausebel, F., R. Brent, R. Kingston, D. Moore, J. G. Seidman, et al. 1989. Current protocols in molecular biology. Wiley, New York, N.Y.
   Google Scholar
• Ballinger, C. A., P. Connell, Y. Wu, Z. Hu, L. J. Thompson, L. Y. Yin, and C. Patterson. 1999. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19: 4535–4545.
   PubMed Web of Science ®Google Scholar
• Becker, J., W. Walter, W. Yan, and E. A. Craig. 1996. Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo. Mol. Cell. Biol. 16: 4378–4386.
   PubMed Web of Science ®Google Scholar
• Boisrame, A., J. M. Beckerich, and C. Gaillardin. 1996. Sls1p, an endoplasmic reticulum component, is involved in the protein translocation process in the yeast Yarrowia lipolytica. J. Biol. Chem. 271: 11668–11675.
   PubMedGoogle Scholar
• Boisrame, A., M. Kabani, J. M. Beckerich, E. Hartmann, and C. Gaillardin. 1998. Interaction of Kar2p and Sls1p is required for efficient co-translational translocation of secreted proteins in the yeast Yarrowia lipolytica. J. Biol. Chem. 273: 30903–30908.
   PubMedGoogle Scholar
• Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14: 115–132.
   PubMed Web of Science ®Google Scholar
• Brehmer, D., S. Rudiger, C. S. Gassler, D. Klostermeier, L. Packschies, J. Reinstein, M. P. Mayer, and B. Bukau. 2001. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nat. Struct. Biol. 8: 427–432.
   PubMedGoogle Scholar
• Briknarova, K., S. Takayama, L. Brive, M. L. Havert, D. A. Knee, J. Velasco, S. Homma, E. Cabezas, J. Stuart, D. W. Hoyt, A. C. Satterthwait, M. Llinas, J. C. Reed, and K. R. Ely. 2001. Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Nat. Struct. Biol. 8: 349–352.
   PubMedGoogle Scholar
• Brodsky, J. L., M. Bauerle, M. Horst, and A. J. McClellan. 1998. Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum. FEBS Lett. 435: 183–186.
   PubMedGoogle Scholar
• Brodsky, J. L., J. Goeckeler, and R. Schekman. 1995. BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92: 9643–9646.
   PubMedGoogle Scholar
• Brodsky, J. L., J. G. Lawrence, and A. J. Caplan. 1998. Mutations in the cytosolic DnaJ homologue, YDJ1, delay and compromise the efficient translation of heterologous proteins in yeast. Biochemistry 37: 18045–18055.
   PubMedGoogle Scholar
• Brodsky, J. L., E. D. Werner, M. E. Dubas, J. L. Goeckeler, K. B. Kruse, and A. A. McCracken. 1999. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274: 3453–3460.
   PubMed Web of Science ®Google Scholar
• Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351–366.
   PubMed Web of Science ®Google Scholar
• Caplan, A. J., D. M. Cyr, and M. G. Douglas. 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71: 1143–1155.
   PubMed Web of Science ®Google Scholar
• Chirico, W. J., M. G. Waters, and G. Blobel. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332: 805–810.
   PubMed Web of Science ®Google Scholar
• Cyr, D. M., and M. G. Douglas. 1994. Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1. J. Biol. Chem. 269: 9798–9804.
   PubMed Web of Science ®Google Scholar
• Cyr, D. M., X. Lu, and M. G. Douglas. 1992. Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267: 20927–20931.
   PubMed Web of Science ®Google Scholar
• Deshaies, R. J., B. D. Koch, M. Werner-Washburne, E. A. Craig, and R. Schekman. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800–805.
   PubMed Web of Science ®Google Scholar
• Fewell, S. W., K. J. Travers, J. S. Weissman, and J. L. Brodsky. 2001. The action of molecular chaperones in the early secretory pathway. Annu. Rev. Genet. 35: 149–191.
   PubMed Web of Science ®Google Scholar
• Frydman, J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70: 603–647.
   PubMed Web of Science ®Google Scholar
• Gässler, C. S., A. Buchberger, T. Laufen, M. P. Mayer, H. Schröder, A. Valencia, and B. Bukau. 1998. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc. Natl. Acad. Sci. USA 95: 15229–15234.
   PubMedGoogle Scholar
• Gässler, C. S., T. Wiederkehr, D. Brehmer, B. Bukau, and M. P. Mayer. 2001. Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J. Biol. Chem. 276: 32538–32544.
   PubMedGoogle Scholar
• Gavin, A. C., M. Bosche, R. Krause, P. Grandi, M. Marzioch, A. Bauer, J. Schultz, J. M. Rick, A. M. Michon, C. M. Cruciat, M. Remor, C. Hofert, M. Schelder, M. Brajenovic, H. Ruffner, A. Merino, K. Klein, M. Hudak, D. Dickson, T. Rudi, V. Gnau, A. Bauch, S. Bastuck, B. Huhse, C. Leutwein, M. A. Heurtier, R. R. Copley, A. Edelmann, E. Querfurth, V. Rybin, G. Drewes, M. Raida, T. Bouwmeester, P. Bork, B. Seraphin, B. Kuster, G. Neubauer, and G. Superti-Furga. 2002. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141–147.
   PubMed Web of Science ®Google Scholar
• Gething, M. J. 1999. Role and regulation of the ER chaperone BiP. Semin. Cell Dev. Biol. 10: 465–472.
   PubMed Web of Science ®Google Scholar
• Harrison, C. J., M. Hayer-Hartl, M. Di Liberto, F. Hartl, and J. Kuriyan. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276: 431–435.
   PubMed Web of Science ®Google Scholar
• Höhfeld, J. 1998. Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights. Biol. Chem. 379: 269–274.
   PubMed Web of Science ®Google Scholar
• Höhfeld, J., and S. Jentsch. 1997. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16: 6209–6216. (Erratum, 17: 847, 1998.)
   PubMed Web of Science ®Google Scholar
• Höhfeld, J., Y. Minami, and F. U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589–598.
   PubMed Web of Science ®Google Scholar
• Horton, L. E., P. James, E. A. Craig, and J. O. Hensold. 2001. The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. J. Biol. Chem. 276: 14426–14433.
   PubMedGoogle Scholar
• Kabani, M., J. M. Beckerich, and C. Gaillardin. 2000. Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol. Cell. Biol. 20: 6923–6934.
   PubMed Web of Science ®Google Scholar
• Kabani, M., A. Boisrame, J. M. Beckerich, and C. Gaillardin. 2000. A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica. Gene 241: 309–315.
   PubMedGoogle Scholar
• Kelley, W. L. 1998. The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci. 23: 222–227.
   PubMed Web of Science ®Google Scholar
• Kelley, W. L., D. M. Cyr, and M. G. Douglas. 1999. Molecular chaperones: how J domains turn on Hsp70s. Curr. Biol. 9: R305–R308.
   PubMed Web of Science ®Google Scholar
• Kim, S., B. Schilke, E. A. Craig, and A. L. Horwich. 1998. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc. Natl. Acad. Sci. USA 95: 12860–12865.
   PubMedGoogle Scholar
• Levy, E. J., J. McCarty, B. Bukau, and W. J. Chirico. 1995. Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators. FEBS Lett. 368: 435–440.
   PubMedGoogle Scholar
• Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88: 2874–2878.
   PubMed Web of Science ®Google Scholar
• Liu, Q., J. Krzewska, K. Liberek, and E. A. Craig. 2001. Mitochondrial Hsp70 Ssc1: role in protein folding. J. Biol. Chem. 276: 6112–6118.
   PubMed Web of Science ®Google Scholar
• Longtine, M. S., A. McKenzie III, D. J. Demarini, N. G. Shah, A. Wach, A. Brachat, P. Philippsen, and J. R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14: 953–961.
   PubMed Web of Science ®Google Scholar
• Lu, Z., and D. M. Cyr. 1998. Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273: 27824–27830.
   PubMed Web of Science ®Google Scholar
• Mally, A., and S. N. Witt. 2001. GrpE accelerates peptide binding and release from the high affinity state of DnaK. Nat. Struct. Biol. 8: 254–257.
   PubMedGoogle Scholar
• McCarty, J. S., A. Buchberger, J. Reinstein, and B. Bukau. 1995. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249: 126–137.
   PubMed Web of Science ®Google Scholar
• McClellan, A. J., and J. L. Brodsky. 2000. 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. Genetics 156: 501–512.
   PubMedGoogle Scholar
• McClellan, A. J., J. B. Endres, J. P. Vogel, D. Palazzi, M. D. Rose, and J. L. Brodsky. 1998. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. Mol. Biol. Cell 9: 3533–3545.
   PubMedGoogle Scholar
• McCracken, A. A., and J. L. Brodsky. 1996. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132: 291–298.
   PubMed Web of Science ®Google Scholar
• Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156: 119–122.
   PubMed Web of Science ®Google Scholar
• Mutka, S. C., and P. Walter. 2001. Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. Mol. Biol. Cell 12: 577–588.
   PubMedGoogle Scholar
• Nelson, R. J., T. Ziegelhoffer, C. Nicolet, M. Werner-Washburne, and E. A. Craig. 1992. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71: 97–105.
   PubMedGoogle Scholar
• Nishikawa, S. I., S. W. Fewell, Y. Kato, J. L. Brodsky, and T. Endo. 2001. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J. Cell Biol. 153: 1061–1070.
   PubMed Web of Science ®Google Scholar
• Ogg, S. C., and P. Walter. 1995. SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation. Cell 81: 1075–1084.
   PubMedGoogle Scholar
• Pfund, C., N. Lopez-Hoyo, T. Ziegelhoffer, B. A. Schilke, P. Lopez-Buesa, W. A. Walter, M. Wiedmann, and E. A. Craig. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17: 3981–3989.
   PubMedGoogle Scholar
• Pierpaoli, E. V., E. Sandmeier, H. J. Schonfeld, and P. Christen. 1998. Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrpE. J. Biol. Chem. 273: 6643–6649.
   PubMedGoogle Scholar
• Raynes, D. A., and V. Guerriero, Jr. 1998. Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. J. Biol. Chem. 273: 32883–32888.
   PubMed Web of Science ®Google Scholar
• Rothblatt, J. A., R. J. Deshaies, S. L. Sanders, G. Daum, and R. Schekman. 1989. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109: 2641–2652.
   PubMedGoogle Scholar
• Sanders, S. L., K. M. Whitfield, J. P. Vogel, M. D. Rose, and R. W. Schekman. 1992. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69: 353–365.
   PubMed Web of Science ®Google Scholar
• Schmid, D., A. Baici, H. Gehring, and P. Christen. 1994. Kinetics of molecular chaperone action. Science 263: 971–973.
   PubMed Web of Science ®Google Scholar
• Shlomai, J., and A. Kornberg. 1980. A prepriming DNA replication enzyme of Escherichia coli. II. Actions of protein n′: a sequence-specific, DNA-dependent ATPase. J. Biol. Chem. 255: 6794–6798.
   PubMed Web of Science ®Google Scholar
• Sondermann, H., C. Scheufler, C. Schneider, J. Hohfeld, F. U. Hartl, and I. Moarefi. 2001. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291: 1553–1557.
   PubMed Web of Science ®Google Scholar
• Stirling, C. J., J. Rothblatt, M. Hosobuchi, R. Deshaies, and R. Schekman. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3: 129–142.
   PubMedGoogle Scholar
• Suh, W. C., W. F. Burkholder, C. Z. Lu, X. Zhao, M. E. Gottesman, and C. A. Gross. 1998. Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc. Natl. Acad. Sci. USA 95: 15223–15228.
   PubMed Web of Science ®Google Scholar
• Suh, W. C., C. Z. Lu, and C. A. Gross. 1999. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274: 30534–30539.
   PubMed Web of Science ®Google Scholar
• Sullivan, C. S., J. D. Tremblay, S. W. Fewell, J. A. Lewis, J. L. Brodsky, and J. M. Pipas. 2000. Species-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40. Mol. Cell. Biol. 20: 5749–5757.
   PubMedGoogle Scholar
• Takayama, S., J. C. Reed, V. R. Agashe, and F. U. Hartl. 2001. Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell Biol. 3: E237–E241.
   PubMed Web of Science ®Google Scholar
• Travers, K. J., C. K. Patil, L. Wodicka, D. J. Lockhart, J. S. Weissman, and P. Walter. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249–258.
   PubMed Web of Science ®Google Scholar
• Tyson, J. R., and C. J. Stirling. 2000. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J. 19: 6440–6452.
   PubMed Web of Science ®Google Scholar
• Ungewickell, E., H. Ungewickell, S. E. Holstein, R. Lindner, K. Prasad, W. Barouch, B. Martin, L. E. Greene, and E. Eisenberg. 1995. Role of auxilin in uncoating clathrin-coated vesicles. Nature 378: 632–635.
   PubMed Web of Science ®Google Scholar
• Werner, E. D., J. L. Brodsky, and A. A. McCracken. 1996. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93: 13797–13801.
   PubMed Web of Science ®Google Scholar
• Yan, W., and E. A. Craig. 1999. The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol. Cell. Biol. 19: 7751–7758.
   PubMed Web of Science ®Google Scholar
• Yan, W., B. Schilke, C. Pfund, W. Walter, S. Kim, and E. A. Craig. 1998. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17: 4809–4817.
   PubMed Web of Science ®Google Scholar
• Zhang, Y., S. Michaelis, and J. L. Brodsky. 2002. CFTR expression and ER associated degradation in yeast. Cystic fibrosis methods and protocols, p. 257–265. In W. R. Skach (ed.). Methods in molecular medicine. Humana Press, Totowa, N.J.
   PubMedGoogle Scholar
• Zhang, Y., G. Nijbroek, M. L. Sullivan, A. A. McCracken, S. C. Watkins, S. Michaelis, and J. L. Brodsky. 2001. Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol. Biol. Cell 12: 1303–1314.
   PubMed Web of Science ®Google Scholar
• Zhong, T., and K. T. Arndt. 1993. The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation. Cell 73: 1175–1186.
   PubMed Web of Science ®Google Scholar
• Zhu, X., X. Zhao, W. F. Burkholder, A. Gragerov, C. M. Ogata, M. E. Gottesman, and W. A. Hendrickson. 1996. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272: 1606–1614.
   PubMed Web of Science ®Google Scholar
• Ziegelhoffer, T., P. Lopez-Buesa, and E. A. Craig. 1995. The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J. Biol. Chem. 270: 10412–10419.
   PubMedGoogle Scholar