ArticleMolecular microbiology2011
Genetic mapping of the interface between the ArsD metallochaperone and the ArsA ATPase.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Heterologous Systems in the Functional Characterization of Proteins from Phytopathogenic Fungi: A Systematic Review.Molecular biotechnology · 2026Article
- Whole-cell bioreporter technology: a promising approach for environmental risk assessment of As contamination in soil.Frontiers in microbiology · 2024Article
- Microbial biochemical pathways of arsenic biotransformation and their application for bioremediation.Folia microbiologica · 2023Review
- Genome sequence ofHeliyon · 2022Article
- ArxA FromFrontiers in microbiology · 2019Article
- Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2014Article
- Evaluative profiling of arsenic sensing and regulatory systems in the human microbiome project genomes.Microbiology insights · 2014Article
- Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Efflux permease CgAcr3-1 of Corynebacterium glutamicum is an arsenite-specific antiporter.The Journal of biological chemistry · 2012Article
- Pathways of arsenic uptake and efflux.Current topics in membranes · 2012Article
- The ArsD As(III) metallochaperone.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2011Article
- As(III) S-adenosylmethionine methyltransferases and other arsenic binding proteins.Geomicrobiology journalArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The ArsD metallochaperone delivers trivalent metalloids, As(III) or Sb(III), to the ArsA ATPase, the catalytic subunit of the ArsAB As(III) efflux pump. Transfer of As(III) increases the affinity of ArsA for As(III), allowing resistance to environmental arsenic concentrations. As(III) transfer is channelled from chaperone to ATPase, implying that ArsD and ArsA form an interface at their metal binding sites. A genetic approach was used to test this hypothesis. Thirteen ArsD mutants exhibiting either weaker or stronger interaction with ArsA were selected by either repressed transactivator yeast two-hybrid or reverse yeast two-hybrid assays. Additionally, Lys-37 and Lys-62 were identified as being involved in ArsD function by site-directed mutagenesis and chemical modification. Substitution at either position with arginine was tolerated, suggesting participation of a positive charge. By yeast two-hybrid analysis K37A and K62A mutants lost interaction with ArsA. All 15 mutations were mapped on the surface of the ArsD structure, and their locations are consistent with a structural model generated by in silico docking. Four are close to metalloid binding site residues Cys-12, Cys-13 and Cys-18, and seven are on the surface of helix 1. These results suggest that the interface involves one surface of helix 1 and the metalloid binding site.
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