Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange
Article Abstract:
The katA gene present in Campylobacter jejuni produces a catalase which protects the bacterial cell from oxidative stress by converting H2O2 to H20 and O2. Campylobacter coli mutants, which do not produce catalase, are unable to detoxify H2O2 being highly sensitive to oxidative stress. The catalase of C. jejuni shows only hydroperoxidase activity and the structure and enzymatic activity of this catalase are similar to the hydroperoxidases produced by other bacteria. The C. coli mutant is formed by allelic exchange between DNA of different origin and katA has an insertion which makes the gene inactive.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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The Bacillus subtilis 168 chromosome from sspE to katA
Article Abstract:
A 24.5 kb region of the Baccillus subtilis 168 chromosome spanning the sspE and katA genes was cloned and sequenced to determine the genomic characteristics of the region. Results show that the region contains a ribosomal RNA operon, rrnD, a tRNA gene set, trnD and 17 ORFs. Sixteen of these ORFs have putative ribosome-binding sites while four match to known B. subtilis genes. Eight of the remaining ORF products show similarities with proteins such as ATP-binding transport protein and a glutamate-1-semialdehyde aminotransferase.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Enterochelin acquisition in Campylobacter coli: characterization of components of a binding-protein-dependent transport system
Article Abstract:
The proteins encoded by the ceuBCDE operon of Campylobacter (C.) coli form a binding-protein-dependent transport system for the uptake of enterochelin. The CeuE protein is the periplasmic protein which binds to enterochelin. CeuB and CeuC are the integral membrane proteins and CeuD is the ATP-binding protein. C. coli cells with a mutation in the ceuBCDE operon show defects in enterochelin uptake and growth. Growth in the ceuD and ceuBCD mutants is stimulated at high concentrations of enterochelin.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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