Literature DB >> 26247431

Functionality of Class A and Class B J-protein co-chaperones with Hsp70.

Hyun Young Yu1, Thomas Ziegelhoffer1, Elizabeth A Craig2.   

Abstract

At their C-termini, cytosolic Hsp70s have an EEVD tetrapeptide that interacts with J-protein co-chaperones of the B, but not A, class. This interaction is required for partnering with yeast B-type J-proteins in protein folding. Here we report conservation of this feature. Human B-type J-proteins also have a stringent EEVD requirement. Human A-type J-proteins function less well than their yeast orthologs with Hsp70ΔEEVD. Changes in the zinc binding domain, a domain absent in B-type J-proteins, overcomes this partial EEVD dependence. Our results suggest that the structurally similar A- and B-class J-proteins of the cytosol have evolved conserved, yet distinct, features that enhance specialized functionality of Hsp70 machinery.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  EEVD motif; Hsp40; Hsp70; Molecular chaperone; Protein folding; Zinc binding domain

Mesh：

Substances：

Year:  2015        PMID： 26247431      PMCID： PMC4570866          DOI： 10.1016/j.febslet.2015.07.040

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


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