Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Panaretou, Barry, Siligardi, Giuliana, Meyer, Philippe, Maloney, Alison, Sullivan, Janis K, Singh, Shradha, Millson, Stefan H, Clarke, Paul A, Naaby-Hansen, Soren, Stein, Rob, Cramer, Rainer, Mollapour, Mehdi, Workman, Paul, Piper, Peter W, Pearl, Laurence H and Prodromou, Chrisostomos (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Molecular Cell, 10 (6). pp. 1307-1318. ISSN 1097-2765

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Abstract

Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are poorly defined. A ubiquitous family of stress-regulated proteins have been identified (Aha1, activator of Hsp90 ATPase) that bind directly to Hsp90 and are required for the in vivo Hsp90-dependent activation of clients such as v-Src, implicating them as cochaperones of the Hsp90 system. In vitro, Aha1 and its shorter homolog, Hch1, stimulate the inherent ATPase activity of yeast and human Hsp90. The identification of these Hsp90 cochaperone activators adds to the complex roles of cochaperones in regulating the ATPase-coupled conformational changes of the Hsp90 chaperone cycle.

Item Type: Article
Keywords: Adenosine Triphosphatases/*metabolism Cell Line, Transformed Centromere/genetics Circular Dichroism Cloning, Molecular Genes, src Genetic Vectors HSP90 Heat-Shock Proteins/genetics/*metabolism Humans Kinetics Molecular Chaperones/chemistry/*genetics/*metabolism Oligonucleotide Array Sequence Analysis Oncogene Protein pp60(v-src)/metabolism Phenotype Recombinant Proteins/metabolism Saccharomyces cerevisiae/genetics/physiology Saccharomyces cerevisiae Proteins/chemistry/*genetics/*metabolism
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Q Science > QH Natural history > QH0301 Biology > QH0426 Genetics
Q Science > QH Natural history > QH0301 Biology
Depositing User: Chrisostomos Prodromou
Date Deposited: 25 Feb 2015 07:18
Last Modified: 06 Mar 2017 17:02
URI: http://sro.sussex.ac.uk/id/eprint/44349

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