http://purl.uniprot.org/citations/19696785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19696785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19696785 | http://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/19696785 | http://purl.org/dc/terms/identifier | "doi:10.1038/embor.2009.153"xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.org/dc/terms/identifier | "doi:10.1038/embor.2009.153"xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Kessler H."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Kessler H."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Stahl M."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Stahl M."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Beck J."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Beck J."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Buchner J."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Buchner J."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Eberl H.C."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Eberl H.C."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Lagleder S."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Lagleder S."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Retzlaff M."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/author | "Retzlaff M."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/name | "EMBO Rep."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/name | "EMBO Rep."xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/pages | "1147-1153"xsd:string |
http://purl.uniprot.org/citations/19696785 | http://purl.uniprot.org/core/pages | "1147-1153"xsd:string |