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Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions

Hennessy, Fritha and Nicoll, Williams S and Zimmermann, Richard and Cheetham, Michael E and Blatch, Gregory L (2005) Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Science, 14 (7). pp. 1697-1709. ISSN 0961-8368

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Abstract

Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that are key components of cellular chaperone networks involved in facilitating the correct folding of a broad range of client proteins. While the Hsp40 family of proteins is highly diverse with multiple forms occurring in any particular cell or compartment, all its members are characterized by a J domain that directs their interaction with a partner Hsp70. Specific Hsp40–Hsp70 chaperone partnerships have been identified that are dedicated to the correct folding of distinct subsets of client proteins. The elucidation of the mechanism by which these specific Hsp40–Hsp70 partnerships are formed will greatly enhance our understanding of the way in which chaperone pathways are integrated into finely regulated protein folding networks. From in silico analyses, domain swapping and rational protein engineering experiments, evidence has accumulated that indicates that J domains contain key specificity determinants. This review will critically discuss the current understanding of the structural features of J domains that determine the specificity of interaction between Hsp40 proteins and their partner Hsp70s. We also propose a model in which the J domain is able to integrate specificity and chaperone activity.

Item Type: Article
Additional Information:

Online ISSN: 1469-896X

Uncontrolled Keywords: ResPubID22214. heat shock proteins, J domain, DnaJ, Hsp70s, Hsp40s, specificity determinants, DnaK
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 0601 Biochemistry and Cell Biology
FOR Classification > 0604 Genetics
Depositing User: VUIR
Date Deposited: 22 Dec 2011 02:28
Last Modified: 29 Jan 2015 03:31
URI: http://vuir.vu.edu.au/id/eprint/8159
DOI: 10.1110/ps.051406805
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Citations in Scopus: 97 - View on Scopus

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