ArticleMolecular microbiology2021
Functional and structural characterization of AntR, an Sb(III) responsive transcriptional repressor.
Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- A DNA damage-activated kinase phosphorylates a transcriptional repressor to control bacterial immune pathway expression.The EMBO journal · 2026Article
- A DNA damage-activated kinase controls bacterial immune pathway expression.bioRxiv : the preprint server for biology · 2026Article
- Repurposing the Sb(III)-specific efflux and sequestration system (ant operon) to mitigate antimonite cross-talk in ArsR-based bacterial arsenite sensors.Microbial cell factories · 2025Article
- Detection of environmental pollutants using transcription factor-based whole-cell biosensors.Biotechnology for the environment · 2025Review
- Mechanisms of genotoxicity and proteotoxicity induced by the metalloids arsenic and antimony.Cellular and molecular life sciences : CMLS · 2023Review
- A Novel Whole-Cell Biosensor for Bioavailable Antimonite in Water and Sediments.Applied and environmental microbiology · 2023Article
- Identification of a MarR Subfamily That Regulates Arsenic Resistance Genes.Applied and environmental microbiology · 2021Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The ant operon of the antimony-mining bacterium Comamonas testosterone JL40 confers resistance to Sb(III). The operon is transcriptionally regulated by the product of the first gene in the operon, antR. AntR is a member of ArsR/SmtB family of metal/metalloid-responsive repressors resistance. We purified and characterized C. testosterone AntR and demonstrated that it responds to metalloids in the order Sb(III) = methylarsenite (MAs(III) >> As(III)). The protein was crystallized, and the structure was solved at 2.1 Å resolution. The homodimeric structure of AntR adopts a classical ArsR/SmtB topology architecture. The protein has five cysteine residues, of which Cys103
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Registered trials
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