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Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch.

Abstract：

:Hsp70 chaperones assist protein folding by reversible interaction with extended hydrophobic segments of substrate polypeptides. We investigated the contribution of three structural elements of the substrate- binding cavity of the Escherichia coli homologue, DnaK, to substrate specificity by investigating mutant DnaK proteins for binding to cellulose-bound peptides. Deletion of the C-terminal subdomain (Delta539-638) and blockage of the access to the hydrophobic pocket in the substrate-binding cavity (V436F) did not change the specificity, although the latter exchange reduced the affinity to all peptides investigated. Mutations (A429W, M404A/A429W) that affect the formation of a hydrophobic arch spanning over the bound substrate disfavored DnaK binding, especially to peptides with short stretches of consecutive hydrophobic residues flanked by acidic residues, while binding to most other peptides remained unchanged. The arch thus contributes to the substrate specificity of DnaK. This finding is of particular interest, since of all the residues of the substrate-binding cavity that contact bound substrate, only the arch-forming residues show significant variation within the Hsp70 family.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Rüdiger S,Mayer MP,Schneider-Mergener J,Bukau B

doi

10.1006/jmbi.2000.4193

keywords:

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

245-51

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)94193-7

journal_volume

304

pub_type

杂志文章

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