ArticleACS chemical biology2015
An alternate pathway of arsenate resistance in E. coli mediated by the glutathione S-transferase GstB.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Distinct bacterial community structures and arsenic biotransformation gene profiles in dust.Frontiers in microbiology · 2025Article
- AsgeneDB: a curated orthology arsenic metabolism gene database and computational tool for metagenome annotation.NAR genomics and bioinformatics · 2022Article
- Glutathione Is Involved in the Reduction of Methylarsenate to Generate Antibiotic Methylarsenite in Enterobacter sp. Strain CZ-1.Applied and environmental microbiology · 2022Article
- Gossypol detoxification in the rumen andAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2021Review
- An arsRB resistance operon confers tolerance to arsenite in the environmental isolate Terribacillus sp. AE2B 122.FEMS microbiology ecology · 2021Article
- Structural and biochemical characterization of a glutathione transferase from the citrus canker pathogen Xanthomonas.Acta crystallographica. Section D, Structural biology · 2020Article
- Functional Role of Tyr12 in the Catalytic Activity of Novel Zeta-like Glutathione S-transferase from Acidovorax sp. KKS102.The protein journal · 2018Article
- Insights Into Arsenite and Arsenate Uptake Pathways Using a Whole Cell Biosensor.Frontiers in microbiology · 2018Article
- Linking Genes to Microbial Biogeochemical Cycling: Lessons from Arsenic.Environmental science & technology · 2017Article
- Genetic Adaptation of Achromobacter sp. during Persistence in the Lungs of Cystic Fibrosis Patients.PloS one · 2015Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
Microbial arsenate resistance is known to be conferred by specialized oxidoreductase enzymes termed arsenate reductases. We carried out a genetic selection on media supplemented with sodium arsenate for multicopy genes that can confer growth to E. coli mutant cells lacking the gene for arsenate reductase (E. coli ΔarsC). We found that overexpression of glutathione S-transferase B (GstB) complemented the ΔarsC allele and conferred growth on media containing up to 5 mM sodium arsenate. Interestingly, unlike wild type E. coli arsenate reductase, arsenate resistance via GstB was not dependent on reducing equivalents provided by glutaredoxins or a catalytic cysteine residue. Instead, two arginine residues, which presumably coordinate the arsenate substrate within the electrophilic binding site of GstB, were found to be critical for transferase activity. We provide biochemical evidence that GstB acts to directly reduce arsenate to arsenite with reduced glutathione (GSH) as the electron donor. Our results reveal a pathway for the detoxification of arsenate in bacteria that hinges on a previously undescribed function of a bacterial glutathione S-transferase.
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