1887

Microbiology

Volume 160, Issue 1

OxyR-dependent expression of a novel glutathione -transferase () gene in DS002 and its role in biotransformation of organophosphate insecticides Free

Abstract

While screening a genomic library of DS002 isolated from organophosphate (OP)-polluted soils, nine ORFs were identified coding for glutathione -transferase (GST)-like proteins. These GSTs (AbGST01–AbGST09) are phylogenetically related to a number of well-characterized GST classes found in taxonomically diverse groups of organisms. Interestingly, expression of (GenBank accession no. KF151191) was upregulated when the bacterium was grown in the presence of an OP insecticide, methyl parathion (MeP). The gene product, AbGST01, dealkylated MeP to desMeP. An OxyR-binding motif was identified directly upstream of . An gene fusion lacking the OxyR-binding site showed a drastic reduction in promoter activity. Very low β-galactosidase activity levels were observed when the fusion was mobilized into an (GenBank accession no. KF151190) null mutant of DS002, confirming the important role of OxyR. The OxyR-binding sites are not found upstream of other () genes. However, they contained consensus sequence motifs that can serve as possible target sites for certain well-characterized transcription factors. In support of this observation, the genes responded differentially to different oxidative stress inducers. The genes identified in DS002 are found to be conserved highly among all known genome sequences of strains. The versatile ecological adaptability of strains is apparent if sequence conservation is seen together with their involvement in detoxification processes.

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2014-01-01
2020-05-27
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OxyR-dependent expression of a novel glutathione S-transferase (Abgst01) gene in Acinetobacter baumannii DS002 and its role in biotransformation of organophosphate insecticides
Microbiology 160, 102 (2014); https://doi.org/10.1099/mic.0.070664-0
/content/journal/micro/10.1099/mic.0.070664-0
/content/journal/micro/10.1099/mic.0.070664-0
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