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ClpE, a novel type of HSP100 ATPase, is part of the CtsR heat shock regulon of Bacillus subtilis
Author(s) -
Derré Isabelle,
Rapoport Georges,
Devine Kevin,
Rose Matthias,
Msadek Tarek
Publication year - 1999
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1999.01374.x
Subject(s) - biology , bacillus subtilis , heat shock protein , gene , regulon , microbiology and biotechnology , atp binding cassette transporter , genetics , bacteria , gene expression , transporter
Clp ATPases, which include the ubiquitous HSP100 family, are classified according to their structural features and sequence similarities. During the course of the Bacillus subtilis genome sequencing project, we identified a gene encoding a new member of the HSP100 family. We designated this protein ClpE, as it is the prototype of a novel subfamily among the Clp ATPases, and have identified homologues in several bacteria, including Listeria monocytogenes , Enterococcus faecalis , Streptococcus pyogenes , Streptococcus pneumoniae , Lactobacillus sakei and Clostridium acetobutylicum . A unique feature of these Hsp100‐type Clp ATPases is their amino‐terminal zinc finger motif. Unlike the other class III genes of B. subtilis ( clpC and clpP ), clpE does not appear to be required for stress tolerance. Transcriptional analysis revealed two σ A ‐type promoters, expression from which was shown to be inducible by heat shock and puromycin treatment. Investigation of the regulatory mechanism controlling clpE expression indicates that this gene is controlled by CtsR and is thus a member of the class III heat shock genes of B. subtilis . CtsR negatively regulates clpE expression by binding to the promoter region, in which five CtsR binding sites were identified through DNase I footprinting and sequence analysis.