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The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae.
FEMS Yeast Res. 2006 Mar; 6(2):195-204.FY

Abstract

Exposure of Saccharomyces cerevisiae to high osmotic stress evokes a number of adaptive changes that are necessary for its survival. These adaptive responses are mediated via multiple mitogen-activated protein kinase pathways, of which the high-osmolarity glycerol (HOG) pathway has been studied most extensively. Yeast strains that bear the hsp82T22I or hsp82G81S mutant alleles are osmosensitive. Interestingly, the osmosensitive phenotype is not due to inappropriate functioning of the HOG pathway, as Hog1p phosphorylation and downstream responses including glycerol accumulation are not affected. Rather, the hsp82 mutants display features that are characteristic for cell-wall mutants, i.e. resistance to Zymolyase and sensitivity to Calcofluor White. The osmosensitivity of the hsp82T22I or hsp82G81S strains is suppressed by over-expression of the Hsp90 co-chaperone Cdc37p but not by other co-chaperones. Hsp90 is shown to be required for proper adaptation to high osmolarity via a novel signal transduction pathway that operates parallel to the HOG pathway and requires Cdc37p.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, Faculty of Science, Vrije Universiteit, Amsterdam, The Netherlands.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16487343

Citation

Yang, Xiao-Xian, et al. "The Molecular Chaperone Hsp90 Is Required for High Osmotic Stress Response in Saccharomyces Cerevisiae." FEMS Yeast Research, vol. 6, no. 2, 2006, pp. 195-204.
Yang XX, Maurer KC, Molanus M, et al. The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. FEMS Yeast Res. 2006;6(2):195-204.
Yang, X. X., Maurer, K. C., Molanus, M., Mager, W. H., Siderius, M., & van der Vies, S. M. (2006). The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. FEMS Yeast Research, 6(2), 195-204.
Yang XX, et al. The Molecular Chaperone Hsp90 Is Required for High Osmotic Stress Response in Saccharomyces Cerevisiae. FEMS Yeast Res. 2006;6(2):195-204. PubMed PMID: 16487343.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. AU - Yang,Xiao-Xian, AU - Maurer,Kick C T, AU - Molanus,Michiel, AU - Mager,Willem H, AU - Siderius,Marco, AU - van der Vies,Saskia M, PY - 2006/2/21/pubmed PY - 2006/5/19/medline PY - 2006/2/21/entrez SP - 195 EP - 204 JF - FEMS yeast research JO - FEMS Yeast Res VL - 6 IS - 2 N2 - Exposure of Saccharomyces cerevisiae to high osmotic stress evokes a number of adaptive changes that are necessary for its survival. These adaptive responses are mediated via multiple mitogen-activated protein kinase pathways, of which the high-osmolarity glycerol (HOG) pathway has been studied most extensively. Yeast strains that bear the hsp82T22I or hsp82G81S mutant alleles are osmosensitive. Interestingly, the osmosensitive phenotype is not due to inappropriate functioning of the HOG pathway, as Hog1p phosphorylation and downstream responses including glycerol accumulation are not affected. Rather, the hsp82 mutants display features that are characteristic for cell-wall mutants, i.e. resistance to Zymolyase and sensitivity to Calcofluor White. The osmosensitivity of the hsp82T22I or hsp82G81S strains is suppressed by over-expression of the Hsp90 co-chaperone Cdc37p but not by other co-chaperones. Hsp90 is shown to be required for proper adaptation to high osmolarity via a novel signal transduction pathway that operates parallel to the HOG pathway and requires Cdc37p. SN - 1567-1356 UR - https://www.unboundmedicine.com/medline/citation/16487343/The_molecular_chaperone_Hsp90_is_required_for_high_osmotic_stress_response_in_Saccharomyces_cerevisiae_ DB - PRIME DP - Unbound Medicine ER -