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A conserved acidic amino acid mediates the interaction between modulators and co-chaperones in enterobacteria.

Abstract：

:Hsp40-like co-chaperones are ubiquitous enzymes that stimulate the protein refolding activity of Hsp70 family chaperones. They are widespread in prokaryotic and eukaryotic systems. In bacteria, the best characterized co-chaperone is the Escherichia coli DnaJ protein. Many γ-proteobacteria encode a functional homologue of DnaJ, known as CbpA, which is expressed in response to starvation and environmental stress. The activity of CbpA is regulated by the "modulator" protein CbpM. Here, we have used a combination of genetics and biochemistry to identify the co-chaperone contact determinant of CbpM. We show that the nature of the interaction is conserved in enterobacteria.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Chintakayala K,Grainger DC

doi

10.1016/j.jmb.2011.05.043

subject

Has Abstract

pub_date

2011-08-12 00:00:00

pages

313-20

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)00606-1

journal_volume

411

pub_type

杂志文章

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