The Burkholderia pseudomallei oxyR gene: expression analysis and mutant characterization

Burkholderia pseudomallei (Bp) is the causative agent of the life-threatening melioidosis in humans. The global transcription factor oxyR gene was isolated and characterized. It is located between recG, encoding a putative DNA helicase, and katG, encoding a putative catalase-peroxidase. oxyR is expr...

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Bibliographic Details
Published in:Gene 2002-08, Vol.296 (1-2), p.161-169
Main Authors: Loprasert, Suvit, Sallabhan, Ratiboot, Whangsuk, Wirongrong, Mongkolsuk, Skorn
Format: Article
Language:English
Subjects:
Bacterial Proteins - genetics
Base Sequence
Biofilms - drug effects
Burkholderia pseudomallei - drug effects
Burkholderia pseudomallei - genetics
Burkholderia pseudomallei - metabolism
Cell Division - drug effects
Cell Division - genetics
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
DNA-Binding Proteins
Dose-Response Relationship, Drug
Endopeptidases - metabolism
Gene Expression Regulation, Bacterial - drug effects
Gene Order
Genetic Complementation Test
Hydrogen Peroxide - pharmacology
Molecular Sequence Data
Mutation
Repressor Proteins - genetics
RNA, Messenger - drug effects
RNA, Messenger - genetics
RNA, Messenger - metabolism
Sequence Analysis, DNA
Transcription Factors - genetics
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Summary:Burkholderia pseudomallei (Bp) is the causative agent of the life-threatening melioidosis in humans. The global transcription factor oxyR gene was isolated and characterized. It is located between recG, encoding a putative DNA helicase, and katG, encoding a putative catalase-peroxidase. oxyR is expressed as a monocistronic 1 kb mRNA and is induced by oxidative stress compounds. Northern, primer extension, and transcription reporter fusion analyses showed that oxyR mRNA is induced by 0.2 mM menadione, 2 mM paraquat, and 10 mM H(2)O(2). Two knockout mutants of oxyR were constructed, by single- and double-crossover recombination, and found to be hypersensitive to H(2)O(2) and paraquat. Bp lacking OxyR exhibited autoaggregation when cultured in liquid broth and an increased ability to form biofilms in minimal medium, but not in Luria-Bertani broth. The oxyR mutants also have a decreased level of extracellular protease activity. The altered phenotypes of oxyR deficient mutants were complemented when a copy of oxyR was transposed into the mutant chromosomes on the mini-Tn5 transposon.
ISSN:0378-1119
DOI:10.1016/S0378-1119(02)00854-5