ArticleNucleic acids research2011
Determinants of redox sensitivity in RsrA, a zinc-containing anti-sigma factor for regulating thiol oxidative stress response.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Metal-responsive RNA polymerase extracytoplasmic function (ECF) sigma factors.Molecular microbiology · 2019Review
- Model peptide for anti-sigma factor domain HHCC zinc fingers: high reactivity towardChemical science · 2019Article
- Structural insights into the regulation of Bacillus subtilis SigW activity by anti-sigma RsiW.PloS one · 2017Article
- Prediction of redox-sensitive cysteines using sequential distance and other sequence-based features.BMC bioinformatics · 2016Article
- Antioxidative responses of Pseudomonas fluorescens YZ2 to simultaneous exposure of Zn and Cefradine.Ecotoxicology (London, England) · 2015Article
- Environmental Sensing in Actinobacteria: a Comprehensive Survey on the Signaling Capacity of This Phylum.Journal of bacteriology · 2015Article
- Thiol-based redox switches in prokaryotes.Biological chemistry · 2015Review
- Redox active thiol sensors of oxidative and nitrosative stress.Antioxidants & redox signaling · 2012Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Various environmental oxidative stresses are sensed by redox-sensitive regulators through cysteine thiol oxidation or modification. A few zinc-containing anti-sigma (ZAS) factors in actinomycetes have been reported to respond sensitively to thiol oxidation, among which RsrA from Streptomyces coelicolor is best characterized. It forms disulfide bonds upon oxidation and releases bound SigR to activate thiol oxidative stress response genes. Even though numerous ZAS proteins exist in bacteria, features that confer redox sensitivity to a subset of these have been uncharacterized. In this study, we identified seven additional redox-sensitive ZAS factors from actinomycetes. Comparison with redox-insensitive ZAS revealed characteristic sequence patterns. Domain swapping demonstrated the significance of the region K(33)FEHH(37)FEEC(41)SPC(44)LEK(47) that encompass the conserved HX(3)CX(2)C (HCC) motif. Mutational effect of each residue on diamide responsive induction of SigR target genes in vivo demonstrated that several residues, especially those that flank two cysteines (E39, E40, L45, E46), contribute to redox sensitivity. These residues are well conserved among redox-sensitive ZAS factors, and hence are proposed as redox-determinants in sensitive ZAS. H37A, C41A, C44A and F38A mutations, in contrast, compromised SigR-binding activity significantly, apparently affecting structural integrity of RsrA. The residue pattern around HCC motif could therefore serve as an indicator to predict redox-sensitive ZAS factors from sequence information.
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