Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast

REFERENCES

• Abbas-Terki, T., O. Donzé, and D. Picard. 2000. The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. FEBS Lett. 467:111–116.
   PubMedGoogle Scholar
• Blum, H. E., H. Beier, and H. J. Gross. 1987. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93–99.
   Web of Science ®Google Scholar
• Bohen, S. P.. 1998. Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins. Mol. Cell. Biol. 18:3330–3339.
   PubMedGoogle Scholar
• Borkovich, K. A., F. W. Farrelly, D. B. Finkelstein, J. Taulien, and S. Lindquist. 1989. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9:3919–3930.
   PubMed Web of Science ®Google Scholar
• Bose, S., T. Weikl, H. Bügl, and J. Buchner. 1996. Chaperone function of Hsp90-associated proteins. Science 274:1715–1717.
   PubMed Web of Science ®Google Scholar
• Buchner, J.. 1999. Hsp90 & Co. — a holding for folding. Trends Biochem. Sci. 24:136–141.
   PubMed Web of Science ®Google Scholar
• Caplan, A. J.. 1999. Hsp90's secrets unfold: new insights from structural and functional studies. Trends Cell Biol. 9:262–268.
   PubMedGoogle Scholar
• Carlson, M.. 1999. Glucose repression in yeast. Curr. Opin. Microbiol. 2:202–207.
   PubMed Web of Science ®Google Scholar
• Chen, S., V. Prapapanich, R. A. Rimerman, B. Honoré, and D. F. Smith. 1996. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70. Mol. Endocrinol. 10:682–693.
   PubMedGoogle Scholar
• Chen, S., and D. F. Smith. 1998. Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J. Biol. Chem. 273:35194–35200.
   PubMedGoogle Scholar
• Chernoff, Y. O., S. L. Lindquist, B. Ono, S. G. Inge-Vechtomov, and S. W. Liebman. 1995. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268:880–884.
   PubMed Web of Science ®Google Scholar
• Cheung, J., and D. F. Smith. 2000. Molecular chaperone interactions with steroid receptors: an update. Mol. Endocrinol. 14:939–946.
   PubMed Web of Science ®Google Scholar
• Connell, P., C. A. Ballinger, J. Jiang, Y. Wu, L. J. Thompson, J. Hohfeld, and C. Patterson. 2001. The cochaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3:93–96.
   PubMed Web of Science ®Google Scholar
• Dolinski, K., S. Muir, M. Cardenas, and J. Heitman. 1997. All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94:13093–13098.
   PubMedGoogle Scholar
• Dolinski, K. J., M. E. Cardenas, and J. Heitman. 1998. CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol. Cell. Biol. 18:7344–7352.
   PubMedGoogle Scholar
• Donzé, O., T. Abbas-Terki, and D. Picard. 2001. The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J. 20:3771–3780.
   PubMed Web of Science ®Google Scholar
• Donzé, O., and D. Picard. 1999. Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the α subunit of eukaryotic translation initiation factor 2. Mol. Cell. Biol. 19:8422–8432.
   PubMedGoogle Scholar
• Duina, A. A., H.-C. J. Chang, J. A. Marsh, S. Lindquist, and R. F. Gaber. 1996. A cyclophilin function in Hsp90-dependent signal transduction. Science 274:1713–1715.
   PubMed Web of Science ®Google Scholar
• Duina, A. A., J. A. Marsh, and R. F. Gaber. 1996. Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth. Yeast 12:943–952.
   PubMed Web of Science ®Google Scholar
• Fang, Y., A. E. Fliss, J. Rao, and A. J. Caplan. 1998. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23. Mol. Cell. Biol. 18:3727–3734.
   PubMedGoogle Scholar
• Freeman, B. C., S. J. Felts, D. O. Toft, and K. R. Yamamoto. 2000. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 14:422–434.
   PubMed Web of Science ®Google Scholar
• Freeman, B. C., D. O. Toft, and R. I. Morimoto. 1996. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274:1718–1720.
   PubMed Web of Science ®Google Scholar
• Frydman, J., and J. Höhfeld. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22:87–92.
   PubMed Web of Science ®Google Scholar
• Glover, J. R., and S. Lindquist. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73–82.
   PubMed Web of Science ®Google Scholar
• Hu, J., D. O. Toft, and C. Seeger. 1997. Hepadnavirus assembly and reverse transcription require a multicomponent chaperone complex which is incorporated into nucleocapsids. EMBO J. 16:59–68.
   PubMed Web of Science ®Google Scholar
• Kimura, Y., S. L. Rutherford, Y. Miyata, I. Yahara, B. C. Freeman, L. Yue, R. I. Morimoto, and S. Lindquist. 1997. Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes Dev. 11:1775–1785.
   PubMed Web of Science ®Google Scholar
• Lässle, M., G. L. Blatch, V. Kundra, T. Takatori, and B. R. Zetter. 1997. Stress-inducible, murine protein mSTI1. J. Biol. Chem. 272:1876–1884.
   PubMed Web of Science ®Google Scholar
• Lindquist, S., and G. Kim. 1996. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. Natl. Acad. Sci. USA 93:5301–5306.
   PubMed Web of Science ®Google Scholar
• Louvion, J.-F., R. Warth, and D. Picard. 1996. Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl. Acad. Sci. USA 93:13937–13942.
   PubMedGoogle Scholar
• Marsh, J. A., H. M. Kalton, and R. F. Gaber. 1998. Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells. Mol. Cell. Biol. 18:7353–7359.
   PubMedGoogle Scholar
• Mayr, C., K. Richter, H. Lilie, and J. Buchner. 2000. Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from saccharomyces cerevisiae, differ in their functional properties. J. Biol. Chem. 275:34140–34146.
   PubMedGoogle Scholar
• Morano, K. A., and D. J. Thiele. 1999. The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo. EMBO J. 18:5953–5962.
   PubMed Web of Science ®Google Scholar
• Moriyama, H., H. K. Edskes, and R. B. Wickner. 2000. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol. 20:8916–8922.
   PubMed Web of Science ®Google Scholar
• Nicolet, C. M., and E. A. Craig. 1989. Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9:3638–3646.
   PubMed Web of Science ®Google Scholar
• Parsell, D. A., A. S. Kowal, M. A. Singer, and S. Lindquist. 1994. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475–478.
   PubMed Web of Science ®Google Scholar
• Pearl, L. H., and C. Prodromou. 2000. Structure and in vivo function of Hsp90. Curr. Opin. Struct. Biol. 10:46–51.
   PubMedGoogle Scholar
• Pirkl, F., and J. Buchner. 2001. Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J. Mol. Biol. 308:795–806.
   PubMedGoogle Scholar
• Sanchez, Y., and S. L. Lindquist. 1990. HSP104 required for induced thermotolerance. Science 248:1112–1115.
   PubMed Web of Science ®Google Scholar
• Sanchez, Y., D. A. Parsell, J. Taulien, J. L. Vogel, E. A. Craig, and S. Lindquist. 1993. Genetic evidence for a functional relationship between Hsp104 and Hsp70. J. Bacteriol. 175:6484–6491.
   PubMed Web of Science ®Google Scholar
• Sanchez, Y., J. Taulien, K. A. Borkovich, and S. Lindquist. 1992. Hsp104 is required for tolerance to many forms of stress. EMBO J. 11:2357–2364.
   PubMed Web of Science ®Google Scholar
• Scheufler, C., A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F. U. Hartl, and I. Moarefi. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101:199–210.
   PubMed Web of Science ®Google Scholar
• Schirmer, E. C., J. R. Glover, M. A. Singer, and S. Lindquist. 1996. HSP100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem. Sci. 21:289–296.
   PubMed Web of Science ®Google Scholar
• Serio, T. R., and S. L. Lindquist. 2000. Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol. 10:98–105.
   PubMedGoogle Scholar
• Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850–858.
   PubMed Web of Science ®Google Scholar
• Warth, R., P.-A. Briand, and D. Picard. 1997. Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation. Biol. Chem. 378:381–391.
   PubMedGoogle Scholar
• Weikl, T., K. Abelmann, and J. Buchner. 1999. An unstructured C-terminal region of the Hsp90 cochaperone p23 is important for its chaperone function. J. Mol. Biol. 293:685–691.
   PubMedGoogle Scholar