PMID- 10991944
OWN - NLM
STAT- MEDLINE
DCOM- 20010118
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 49
DP  - 2000 Dec 8
TI  - H2O2-sensitive fur-like repressor CatR regulating the major catalase gene in 
      Streptomyces coelicolor.
PG  - 38254-60
AB  - 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 H(2)O(2) and is required for efficient 
      aerobic growth. In order to investigate the H(2)O(2)-dependent regulatory 
      mechanism, an H(2)O(2)-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 H(2)O(2) treatment, suggesting that the repressor 
      activity of CatR may be directly modulated by H(2)O(2). 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 H(2)O(2) 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.
FAU - Hahn, J S
AU  - Hahn JS
AD  - Laboratory of Molecular Microbiology, School of Biological Sciences, and 
      Institute of Microbiology, Seoul National University, Seoul 151-742, Korea.
FAU - Oh, S Y
AU  - Oh SY
FAU - Chater, K F
AU  - Chater KF
FAU - Cho, Y H
AU  - Cho YH
FAU - Roe, J H
AU  - Roe JH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (ferric uptake regulating proteins, bacterial)
RN  - 126124-77-4 (CatR protein, bacteria)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - EC 1.11.1.6 (Catalase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry/*metabolism
MH  - Base Sequence
MH  - Catalase/*genetics
MH  - Cosmids
MH  - DNA-Binding Proteins/chemistry/*genetics/*metabolism
MH  - *Gene Expression Regulation, Bacterial/drug effects
MH  - *Gene Expression Regulation, Enzymologic/drug effects
MH  - Gene Library
MH  - Hydrogen Peroxide/*pharmacology
MH  - Molecular Sequence Data
MH  - Oxidation-Reduction
MH  - Promoter Regions, Genetic
MH  - Repressor Proteins/chemistry/genetics/*metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Sequence Homology, Nucleic Acid
MH  - Streptomyces/*genetics/*metabolism
MH  - Transcription Factors/chemistry/*genetics/*metabolism
MH  - Transcription, Genetic
EDAT- 2000/09/19 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/09/19 11:00
PHST- 2000/09/19 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/09/19 11:00 [entrez]
AID - S0021-9258(19)55951-8 [pii]
AID - 10.1074/jbc.M006079200 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Dec 8;275(49):38254-60. doi: 10.1074/jbc.M006079200.