Construction and analysis of hybrid Escherichia coli-Bacillus subtilis dnaK genes.

Abstract:

:The highly conserved DnaK chaperones consist of an N-terminal ATPase domain, a central substrate-binding domain, and a C-terminal domain whose function is not known. Since Bacillus subtilis dnaK was not able to complement an Escherichia coli dnaK null mutant, we performed domain element swap experiments to identify the regions responsible for this finding. It turned out that the B. subtilis DnaK protein needed approximately normal amounts of the cochaperone DnaJ to be functional in E. coli. The ATPase domain and the substrate-binding domain form a species-specific functional unit, while the C-terminal domains, although less conserved, are exchangeable. Deletion of the C-terminal domain in E. coli DnaK affected neither complementation of growth at high temperatures nor propagation of phage lambda but abolished degradation of sigma32.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Mogk A,Bukau B,Lutz R,Schumann W

doi

10.1128/JB.181.6.1971-1974.1999

keywords:

subject

Has Abstract

pub_date

1999-03-01 00:00:00

pages

1971-4

issue

6

eissn

0021-9193

issn

1098-5530

journal_volume

181

pub_type

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