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	Proc. Natl. Acad. Sci. U.S.A. Apr (2007); 104(17):7163-8
Network of general and specialty J protein chaperones of the yeast cytosol-
Sahi C, Craig EA
Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA-
Abstract: J proteins are obligate cochaperones of Hsp70s, stimulating their ATPase activity and thus allowing them to function in multiple cellular processes- In most cellular compartments, an Hsp70 works with multiple, structurally divergent J proteins- To better understand the functional specificity of J proteins and the complexity of the Hsp70-J protein network, we undertook a comprehensive analysis of 13 J proteins of the cytosol of the yeast Saccharomyces cerevisiae- Phenotypes caused by the absence of four proteins, Sis1, Jjj1, Jjj3, and Cwc23, could not be rescued by overexpression of any other cytosolic J protein, demonstrating the distinctive nature of J proteins- In one case, that of Zuo1, the phenotypic effects of the absence of a J protein could be rescued by overexpression of only one other J protein, Jjj1, which, like Zuo1, is ribosome-associated- In contrast, the severe growth phenotype caused by the absence of the cytosol's most abundant J protein, Ydj1, was substantially rescued by expression of J domain-containing fragments of many cytosolic J proteins- We conclude that many functions of Hsp70 chaperone machineries only require stimulation of Hsp70's ATPase activity by J protein partners- However, a subset of Hsp70 functions requires specific J protein partners, likely demanding either sublocalization within the compartment or binding to specific client proteins-
[PUBMED: 17438278]

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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
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