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http://purl.uniprot.org/citations/19696785http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19696785http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19696785http://www.w3.org/2000/01/rdf-schema#comment"Heat shock protein 90 (Hsp90) is an abundant, dimeric ATP-dependent molecular chaperone, and ATPase activity is essential for its in vivo functions. S-nitrosylation of a residue located in the carboxy-terminal domain has been shown to affect Hsp90 activity in vivo. To understand how variation of a specific amino acid far away from the amino-terminal ATP-binding site regulates Hsp90 functions, we mutated the corresponding residue and analysed yeast and human Hsp90 variants both in vivo and in vitro. Here, we show that this residue is a conserved, strong regulator of Hsp90 functions, including ATP hydrolysis and chaperone activity. Unexpectedly, the variants alter both the C-terminal and N-terminal association properties of Hsp90, and shift its conformational equilibrium within the ATPase cycle. Thus, S-nitrosylation of this residue allows the fast and efficient fine regulation of Hsp90."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.org/dc/terms/identifier"doi:10.1038/embor.2009.153"xsd:string
http://purl.uniprot.org/citations/19696785http://purl.org/dc/terms/identifier"doi:10.1038/embor.2009.153"xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Kessler H."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Kessler H."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Stahl M."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Stahl M."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Beck J."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Beck J."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Buchner J."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Buchner J."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Eberl H.C."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Eberl H.C."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Lagleder S."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Lagleder S."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Retzlaff M."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/author"Retzlaff M."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/name"EMBO Rep."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/name"EMBO Rep."xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/pages"1147-1153"xsd:string
http://purl.uniprot.org/citations/19696785http://purl.uniprot.org/core/pages"1147-1153"xsd:string