ArticleJournal of microbiology (Seoul, Korea)2022
Characterization of components of a reducing system for SoxR in the cytoplasmic membrane of Escherichia coli.
Article in Journal of microbiology (Seoul, Korea), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Mutations in the superoxide-responsive regulator SoxR confer fluoroquinolone resistance inCurrent research in microbial sciences · 2026Article
- The Role of the [2Fe-2S] Cluster of Escherichia coli IscR in Responding to Redox-Cycling Agents.Molecular microbiology · 2025Article
- The RNF/NQR redox pumps: a versatile system for energy transduction in bacteria and archaea.Applied microbiology and biotechnology · 2025Review
- Functional Characterization of RseC in the SoxR Reducing System and Its Role in Oxidative Stress Response inJournal of microbiology and biotechnology · 2024Article
- AcrAB-TolC efflux pump overexpression and tet(A) gene mutation increase tigecycline resistance in Klebsiella pneumoniae.World journal of microbiology & biotechnology · 2024Article
- Functional analysis of bacterial genes accidentally packaged in rhizospheric phageome of the wild plant speciesSaudi journal of biological sciences · 2023Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A reducing system of SoxR, a regulator of redox-active molecules, was identified as rsxABCDGE gene products and RseC in Escherichia coli through genetic studies. We found that ApbE was an additional component of the reducer system. Bacterial two hybrid analysis revealed that these proteins indeed had multiple interactions among themselves. RseC and RsxB formed the core of the complex, interacting with more than five other components. RsxC, the only cytoplasmic component of the system, interacted with SoxR. It might be linked with the rest of the complex via RsxB. Membrane fractions containing the wild type complex but not the mutant complex reduced purified SoxR using NADH as an electron source. These results suggest that Rsx genes, RseC, and ApbE can form a complex using NAD(P)H to reduce SoxR.
Indexed as
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Registered trials
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