Literature DB >> 1336034

The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli.

S L Morris1, J Nair, D A Rouse.   

Abstract

The activation of catalase genes in response to oxidative stress may contribute to the intracellular survival of mycobacteria. In this report, the nucleotide sequence of a mycobacterial catalase gene is described. The deduced protein sequence of this Mycobacterium intracellulare gene (MI85) was 60% identical to the Escherichia coli hydroperoxidase I (HPI) protein, 59% identical to the Salmonella typhimurium (HPI) catalase, and 47% identical to a Bacillus stearothermophilus peroxidase. The MI85 protein, expressed in E. coli, has also been shown to have peroxidase and catalase activities. Furthermore, Southern blot hybridizations, which demonstrated that a MI85 gene probe hybridizes with chromosomal DNA from thirteen different strains of mycobacteria, suggest that this catalase-peroxidase gene is prevalent in the mycobacterial genus. The availability of catalase gene probes should permit an evaluation, at the molecular level, of the role of catalase in mycobacterial pathogenesis.

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Year:  1992        PMID: 1336034     DOI: 10.1099/00221287-138-11-2363

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN: 0022-1287


  12 in total

1.  Nucleotide sequence of the Mycobacterium leprae katG region.

Authors:  N Nakata; M Matsuoka; Y Kashiwabara; N Okada; C Sasakawa
Journal:  J Bacteriol       Date:  1997-05       Impact factor: 3.490

2.  Exploring the structure and function of the mycobacterial KatG protein using trans-dominant mutants.

Authors:  Joseph A DeVito; Sheldon Morris
Journal:  Antimicrob Agents Chemother       Date:  2003-01       Impact factor: 5.191

3.  katGI and katGII encode two different catalases-peroxidases in Mycobacterium fortuitum.

Authors:  M C Menéndez; J A Ainsa; C Martín; M J García
Journal:  J Bacteriol       Date:  1997-11       Impact factor: 3.490

4.  Identification and characterization of a novel extracellular ferric reductase from Mycobacterium paratuberculosis.

Authors:  M Homuth; P Valentin-Weigand; M Rohde; G F Gerlach
Journal:  Infect Immun       Date:  1998-02       Impact factor: 3.441

5.  Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae.

Authors:  M G Klotz; Y C Kim; J Katsuwon; A J Anderson
Journal:  Appl Microbiol Biotechnol       Date:  1995 Aug-Sep       Impact factor: 4.813

6.  The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli.

Authors:  M Mutsuda; T Ishikawa; T Takeda; S Shigeoka
Journal:  Biochem J       Date:  1996-05-15       Impact factor: 3.857

7.  Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis.

Authors:  B Heym; Y Zhang; S Poulet; D Young; S T Cole
Journal:  J Bacteriol       Date:  1993-07       Impact factor: 3.490

8.  Molecular mechanisms of isoniazid resistance in Mycobacterium tuberculosis and Mycobacterium bovis.

Authors:  D A Rouse; S L Morris
Journal:  Infect Immun       Date:  1995-04       Impact factor: 3.441

9.  Characterization of the katG and inhA genes of isoniazid-resistant clinical isolates of Mycobacterium tuberculosis.

Authors:  D A Rouse; Z Li; G H Bai; S L Morris
Journal:  Antimicrob Agents Chemother       Date:  1995-11       Impact factor: 5.191

10.  Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis.

Authors:  E R Rocha; C J Smith
Journal:  J Bacteriol       Date:  1995-06       Impact factor: 3.490

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