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Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae.

Department of Physiological Chemistry, University of Wisconsin-Madison 53706.

ABSTRACT

We have isolated a gene from the yeast Saccharomyces cerevisiae that encodes a 2.0-kilobase heat-inducible mRNA. This gene, which we have designated STI1, for stress inducible, was also induced by the amino acid analog canavanine and showed a slight increase in expression as cells moved into stationary phase. The STI1 gene encodes a 66-kilodalton protein, as determined from the sequence of the longest open reading frame. The putative STI1 protein, as identified by two-dimensional gel electrophoresis, migrated in the region of 73 to 75 kilodaltons as a series of four isoforms with different isoelectric points. STI1 is not homologous to the other conserved HSP70 family members in yeasts, despite similarities in size and regulation. Cells carrying a disruption mutation of the STI1 gene grew normally at 30 degrees C but showed impaired growth at higher and lower temperatures. Overexpression of the STI1 gene resulted in substantial trans-activation of SSA4 promoter-reporter gene fusions, indicating that STI1 may play a role in mediating the heat shock response of some HSP70 genes.

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• Chen, S., Smith, D. F. (1998). Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery. J. Biol. Chem. 273: 35194-35200 [Abstract] [Full Text]  
• Baxter, B. K., Craig, E. A. (1998). Suppression of an Hsp70 Mutant Phenotype in Saccharomyces cerevisiae through Loss of Function of the Chromatin Component Sin1p/Spt2p. J. Bacteriol. 180: 6484-6492 [Abstract] [Full Text]  
• Dolinski, K. J., Cardenas, M. E., Heitman, J. (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 [Abstract] [Full Text]  
• Marsh, J. A., Kalton, H. M., Gaber, R. F. (1998). Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7Delta Cells. Mol. Cell. Biol. 18: 7353-7359 [Abstract] [Full Text]  
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• Johnson, B. D., Schumacher, R. J., Ross, E. D., Toft, D. O. (1998). Hop Modulates hsp70/hsp90 Interactions in Protein Folding. J. Biol. Chem. 273: 3679-3686 [Abstract] [Full Text]  
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• Pratt, W. B., Toft, D. O. (1997). Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones. Endocr. Rev. 18: 306-360 [Abstract] [Full Text]  
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• Irmer, H., Hohfeld, J. (1997). Characterization of Functional Domains of the Eukaryotic Co-chaperone Hip. J. Biol. Chem. 272: 2230-2235 [Abstract] [Full Text]  
• Lassle, M., Blatch, G. L., Kundra, V., Takatori, T., Zetter, B. R. (1997). Stress-inducible, Murine Protein mSTI1. CHARACTERIZATION OF BINDING DOMAINS FOR HEAT SHOCK PROTEINS AND IN VITRO PHOSPHORYLATION BY DIFFERENT KINASES. J. Biol. Chem. 272: 1876-1884 [Abstract] [Full Text]  
• Schneider, C., Sepp-Lorenzino, L., Nimmesgern, E., Ouerfelli, O., Danishefsky, S., Rosen, N., Hartl, F. U. (1996). Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. USA 93: 14536-14541 [Abstract] [Full Text]  
• Gross, M., Hessefort, S. (1996). Purification and Characterization of a 66-kDa Protein from Rabbit Reticulocyte Lysate Which Promotes the Recycling of Hsp 70. J. Biol. Chem. 271: 16833-16841 [Abstract] [Full Text]  
• Gross, M., Hessefort, S., Olin, A., Reddy, G. (1996). Extensive Sequencing of Tryptic Peptides of a Rabbit Reticulocyte 66-kDa Protein That Promotes Recycling of Hsp 70. HOMOLOGY TO STRESS-RELATED PROTEINS. J. Biol. Chem. 271: 16842-16849 [Abstract] [Full Text]  
• Dittmar, K. D., Hutchison, K. A., Owens-Grillo, J. K., Pratt, W. B. (1996). Reconstitution of the Steroid Receptor·hsp90 Heterocomplex Assembly System of Rabbit Reticulocyte Lysate. J. Biol. Chem. 271: 12833-12839 [Abstract] [Full Text]  
• Maillet, I., Lagniel, G., Perrot, M., Boucherie, H., Labarre, J. (1996). Rapid Identification of Yeast Proteins on Two-dimensional Gels. J. Biol. Chem. 271: 10263-10270 [Abstract] [Full Text]  
• Guenette, S, Magendantz, M, Solomon, F (1995). Suppression of a conditional mutation in alpha-tubulin by overexpression of two checkpoint genes. J. Cell Sci. 108: 1195-1204 [Abstract]  
• Zhang, K, Smouse, D, Perrimon, N (1991). The crooked neck gene of Drosophila contains a motif found in a family of yeast cell cycle genes.. Genes Dev. 5: 1080-1091 [Abstract]  
• Murphy, P. J. M., Kanelakis, K. C., Galigniana, M. D., Morishima, Y., Pratt, W. B. (2001). Stoichiometry, Abundance, and Functional Significance of the hsp90/hsp70-based Multiprotein Chaperone Machinery in Reticulocyte Lysate. J. Biol. Chem. 276: 30092-30098 [Abstract] [Full Text]