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J. Biol. Chem., Vol. 275, Issue 49, 38254-38260, December 8, 2000
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From the Streptomyces coelicolor produces
three distinct catalases to cope with oxidative and osmotic stresses
and allow proper growth and differentiation. The major vegetative
catalase A (CatA) is induced by H2O2 and is
required for efficient aerobic growth. In order to investigate the
H2O2-dependent regulatory
mechanism, an H2O2-resistant mutant (HR40)
overproducing CatA was isolated from S. coelicolor A3(2).
Based on the genetic map location of the mutated locus in HR40, the
wild type catR gene was isolated from the ordered cosmid
library of S. coelicolor by screening for its ability to
suppress the HR40 phenotype. catR encodes a protein of 138 amino acids (15319 Da), with sequence homology to ferric uptake
regulator (Fur)-like proteins. Disruption of catR caused
CatA overproduction as observed in the HR40 mutant, confirming the role
of CatR as a negative regulator of catA expression. The
levels of catA and catR transcripts were higher
in HR40 than in the wild type, implying that CatR represses
transcription of these genes. Transcripts from the catA and
catR genes were induced within 10 min of
H2O2 treatment, suggesting that the repressor activity of CatR may be directly modulated by
H2O2. A putative CatR-binding site containing
an inverted repeat of 23 base pairs was localized upstream of
the catA and catR gene, on the basis of
sequence comparison and deletion analysis. CatR protein purified in the
presence of dithiothreitol bound to this region, whereas oxidized CatR,
treated with H2O2 or diamide, did not. The
redox shift of CatR involved thiol-disulfide exchange as judged by
modification of free thiols with
4-acetamido-4'-maleimidylstilbene-2,2'-disulfonate. From these results
we propose that CatR regulates its downstream target genes as a
repressor whose DNA binding ability is directly modulated by redox
changes in the cell.
H2O2-sensitive Fur-like Repressor CatR
Regulating the Major Catalase Gene in Streptomyces
coelicolor*
§¶,
,, and**
Laboratory of Molecular Microbiology, School
of Biological Sciences, and Institute of Microbiology, Seoul National
University, Seoul 151-742, Korea and the § Department of
Genetics, John Innes Centre, Colney,
Norwich NR4 7UH, United Kingdom
*
This work was supported by International Collaborative
Research Grants from Korea Science and Engineering Foundation (KOSEF) and the Biotechnology and Biological Sciences Research Council (BBSRC).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by BK21 Research Fellowship from the Korean Ministry
of Education.
**
To whom correspondence should be addressed. Tel.: 82-2-880-6706;
Fax: 82-2-888-4911; E-mail: jhroe@plaza.snu.ac.kr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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