CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90

Molecular and Cellular Biology

Volumn 18, Issue 12, 1998, Pages 7344-7352

  Dolinski, Kara J ^a   Cardenas, Maria E ^a   Heitman, Joseph ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN; CYCLOSPORIN A; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; PROTEIN KINASE P60;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CYTOTOXICITY; FUNGUS GROWTH; GENE EXPRESSION REGULATION; GENE MUTATION; GENE OVEREXPRESSION; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; SUPPRESSOR GENE;

FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0031756340     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.12.7344     Document Type: Article

References (60)

1. 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.
2. Bohen, S. P., and K. R. Yamamoto. 1994. Modulation of steroid receptor signal transduction by heat shock proteins, p. 313-334. In R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
3. Borkovich, K., 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.
4. Bose, S., T. Weikl, H. Bugl, and J. Buchner. 1996. Chaperone function of Hsp90-associated proteins. Science 274:1715-1717.
5. Botstein, D., S. C. Falco, S. E. Stewart, M. Brennan, S. Scherer, D. T. Stinchcomb, K. Struhl, and R. W. Davis. 1979. Sterile host yeasts (SHY): a eukaryotic system of biological containment for recombinant DNA experiments. Gene 8:17-24.
6. Caplan, A. J. 1997. Yeast molecular chaperones and the mechanism of steroid hormone action. Trends Endocrinol. Metab. 8:271-276.
7. Cardenas, M., C. Hemenway, R. S. Muir, R. Ye, D. Fiorentino, and J. Heitman. 1994. Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands. EMBO J. 13:5944-5957.
8. Chang, H.-C. J., and S. Lindquist. 1994. Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269:24983-24988.
9. Chang, H.-C. J., D. F. Nathan, and S. Lindquist. 1997. In vivo analysis of the Hsp90 cochaperone Stil (p60). Mol. Cell. Biol. 17:318-325.
10. Chen, M.-S., A. M. Silverstein, W. B. Pratt, and M. Chinkers. 1996. The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant. J. Biol. Chem. 271:32315-32320.
11. Cherry, J. M., C. Adler, C. Ball, S. Dwight, S. Chervitz, G. Juvik, T. Roe, S. Weng, and D. Botstein. 1997. Saccharomyces genome database. http: //genome-www.stanford.edu/Saccharomyces/October 9, 1997.
12. Cullin, C., and L. Minvielle-Sebastia. 1994. Multipurpose vectors designed for the fast generation of N-or C-terminal epitope-tagged proteins. Yeast 10:105-112.
13. Das, A. K., P. T. W. Cohen, and D. Barford. 1998. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17:1192-1199.
14. Deshaies, R. J. 1995. Make it or break it: the role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol. 5:428-434.
15. Dolinski, K., R. S. Muir, M. E. 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.
16. Duina, A. A., H. C. Chang, J. A. Marsh, S. Lindquist, and R. F. Gaber. 1996. A cyclophilin function in Hsp-90 dependent signal transduction. Science 274:1713-1715.
17. 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.
18. Duina, A. A., J. A. Marsh, R. B. Kurtz, H.-C. J. Chang, S. Londquist, and R. F. Gaber. 1998. The peptidyl-prolyl isomerase domain of the Cyp-40 cyclophilin 40 homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. J. Biol. Chem. 273: 10819-10822.
19. Fang, Y., A. E. Fliss, J. Rao, and A. J. Caplan. 1998. SBA1 encodes a yeast Hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol. Cell. Biol. 18:3727-3734.
20. Fliss, A. E., Y. Fang, F. Boschelli, and A. J. Caplan. 1997. Differential in vivo regulation of steroid hormone receptor activation by Cdc37p. Mol. Biol. Cell 8:2501-2509.
21. Frangioni, J. V., and B. G. Neel. 1993. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 210:179-187.
22. 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.
23. Gietz, R. D., R. H. Schiestl, A. Willems, and R. A. Woods. 1995. Studies on the mechanism of high efficiency transformation of intact yeast cells. Yeast 11:355-360.
24. Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
25. Godowski, P. J., D. Picard, and K. R. Yamamoto. 1988. Signal transduction and transcriptional regulation by glucocorticoid receptor-LexA fusion proteins. Science 241:812-816.
26. Gaber, R. Personal communication.
27. Grenert, J. P., W. P. Sullivan, P. Fadden, T. A. J. Haystead, J. Clark, E. Mimnaugh, H. Knitzsch, H. J. Ochel, T. W. Schulte, E. Sausville, L. M. Neckers, and D. O. Toft. 1997. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J. Biol. Chem. 272:23843-23850.
28. Heitman, J., N. R. Movva, P. C. Hiestand, and M. N. Hall. 1991. FK506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 88: 1948-1952.
29. Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
30. Hochstrasser, M. 1996. Protein degradation or regulation: Ub the judge. Cell 84:853-862.
31. Hoffman, C. S., and F. Winston. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57:267-272.
32. Kieffer, L. J., T. W. Seng, W. Li, D. G. Osterman, R. E. Handschumacher, and R. M. Bayney. 1993. Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. J. Biol. Chem. 268:12303-12310.
33. 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.
34. Kominami, K.-I., N. Okura, M. Kawamura, G. N. DeMartino, C. A. Slaughter, N. Shimbara, C. H. Chung, M. Fujimuro, H. Yokosawa, Y. Shimizu, N. Tanahashi, K. Tanaka, and A. Toh-e. 1997. Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multi-copy suppressors of nin1-1. Mol. Biol. Cell 8:171-187.
35. Leverson, J. D., and S. A. Ness. 1998. Point mutations in v-myb disrupt a cyclophilin-catalyzed negative regulatory mechanism. Mol. Cell 1:203-211.
36. Lorenz, M. C., R. S. Muir, E. Lim, J. McElver, S. C. Weber, and J. Heitman. 1995. Gene disruption with PCR products in Saccharomyces cerevisiae. Gene 158:113-117.
37. Mak, P., D. P. McDonnell, N. L. Weigel, W. T. Schrader, and B. W. O'Malley. 1989. Expression of functional chicken oviduct progesterone receptors in yeast (Saccharomyces cerevisiae). J. Biol. Chem. 284:21613-21618.
38. Metzger, D., J. H. White, and P. Chambon. 1988. The human oestrogen receptor functions in yeast. Nature 334:31-36.
39. Miao, B., J. Davis, and E. A. Craig. 1997. The Hsp70 family - an overview, p. 3-13. In M.-J. Gething (ed.). Guidebook to molecular chaperones and protein-folding catalysts. Oxford University Press, New York, N.Y.
40. 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.
41. Orr-Weaver, T. L., J. W. Szostak, and R. J. Rothstein. 1981. Yeast transformation: a model system for the study of recombination. Proc. Natl. Acad. Sci. USA 78:6354-6358.
42. Owens-Grillo, J. K., L. F. Stancato, K. Hoffmann, W. B. Pratt, and P. Krishna. 1996. Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants. Biochemistry 35:15249-15255.
43. Picard, D., B. Khursheed, M. J. Garabedian, M. G. Fortin, S. Lindquist, and K. R. Yamamoto. 1990. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348:166-168.
44. Pratt, W. B. 1993. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268: 21455-21458.
45. Ratajczak, T., and A. Carrello. 1996. Cyclophilin 40 (Cyp-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with Cyp-40 for hsp90 binding. J. Biol. Chem. 271:2961-2965.
46. Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281-301.
47. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
48. Schmitt, M. E., T. A. Brown, and B. L. Trumpower. 1990. A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18:3091-3092.
49. Schneider, C., L. Sepp-Lorenzino, E. Nimmesgern, O. Ouerfelli, S. Danishefsky, N. Rosen, and F. U. Hartl. 1996. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. USA 93:14536-14541.
50. Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
51. Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
52. cdc23 of Saccharomyces cerevisiae: a nuclear tetratricopeptide repeat protein with two mutable domains. Mol. Cell. Biol. 13:1212-1221.
53. Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase. Gene 67:31-40.
54. Smith, D. F. 1993. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7:1418-1429.
55. Smith, D. F., L. Whitesell, S. C. Nair, S. Chen, V. Prapapanich, and R. A. Rimerman. 1995. Progesterone receptor structure and function altered by geldanamycin, an Hsp90-binding agent. Mol. Cell. Biol. 15:6804-6812.
56. Stebbins, C. E., A. A. Russo, C. Schneider, N. Rosen, F. U. Hartl, and N. P. Pavletich. 1997. Crystal structure of an Hsp90-geldanamycin complex: targeling of a protein chaperone by an antitumor agent. Cell 89:239-250.
57. Wach, A., A. Brachal, R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10:1793-1808.
58. 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.
59. Weisman, R., J. Creanor, and P. Fantes. 1996. A multicopy suppressor of a cell cycle defect in S. pombe encodes a heat shock-inducible 40 kDa cyclophilin-like protein. EMBO J. 15:447-456.
60. Whitesell, L., E. G. Mimnaugh, B. D. Costa, C. E. Myers, and L. M. Neckers. 1994. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91:8324-8328.