- Characterization of components of a reducing system for SoxR in the cytoplasmic membrane of Escherichia coli
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Kang-Lok Lee , Kyung-Chang Lee , Joon-Hee Lee , Jung-Hye Roe
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J. Microbiol. 2022;60(4):387-394. Published online March 28, 2022
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DOI: https://doi.org/10.1007/s12275-022-1667-1
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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.
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Citations
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- Mutations in the superoxide-responsive regulator SoxR confer fluoroquinolone resistance in Stenotrophomonas maltophilia
Poonyaporn Kanawong, Parinya Tipanyo, Suleepon Poomchuchit, Skorn Mongkolsuk, Paiboon Vattanaviboon, Nisanart Charoenlap Current Research in Microbial Sciences.2026; 10: 100609. CrossRef - The RNF/NQR redox pumps: a versatile system for energy transduction in bacteria and archaea
Wolfgang Buckel, Ulrich Ermler, Janet Vonck, Günter Fritz, Julia Steuber Applied Microbiology and Biotechnology.2025;[Epub] CrossRef - The Role of the [2Fe‐2S] Cluster of Escherichia coli IscR in Responding to Redox‐Cycling Agents
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Zhaoxin Xia, Jing zhou, Nana Gao, Ge Li, Runde Liu, Guoping Lu, Jilu Shen World Journal of Microbiology and Biotechnology.2024;[Epub] CrossRef - The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR): Physiological role, structure and function of a redox-driven, molecular machine
Julia Steuber, Günter Fritz Biochimica et Biophysica Acta (BBA) - Bioenergetics.2024; 1865(4): 149485. CrossRef - Functional Characterization of RseC in the SoxR Reducing System and Its Role in Oxidative Stress Response in Escherichia coli
Kang-Lok Lee, Joon-Hee Lee, Yun-Hee Kim, Jung-Hye Roe Journal of Microbiology and Biotechnology.2024; 34(12): 2547. CrossRef - Functional analysis of bacterial genes accidentally packaged in rhizospheric phageome of the wild plant species Abutilon fruticosum
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- Regulation of iron homeostasis by peroxide-sensitive CatR, a Fur-family regulator in Streptomyces coelicolor
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Yeonbum Kim , Jung-Hye Roe , Joo-Hong Park , Yong-Joon Cho , Kang-Lok Lee
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J. Microbiol. 2021;59(12):1083-1091. Published online December 4, 2021
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DOI: https://doi.org/10.1007/s12275-021-1457-1
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CatR, a peroxide-sensing transcriptional repressor of Fur
family, can de-repress the transcription of the catA gene encoding
catalase upon peroxide stress in Streptomyces coelicolor.
Since CatR-regulated genes other than catA and its own
gene catR have not been identified in detail, the understanding
of the role of CatR regulon is very limited. In this study,
we performed transcriptomic analysis to identify genes influenced
by both atR mutation and hydrogen peroxide treatment.
Through ChIP-qPCR and other analyses, a new consensus
sequence was found in CatR-responsive promoter region
of catR gene and catA operon for direct regulation. In
addition, vtlA (SCO2027) and SCO4983 were identified as new
members of the CatR regulon. Expression levels of iron uptake
genes were reduced by hydrogen peroxide and a DmdR1 binding
sequence was identified in promoters of these genes. The
increase in free iron by hydrogen peroxide was thought to
suppress the iron import system by DmdR1. A putative exporter
protein VtlA regulated by CatR appeared to reduce intracellular
iron to prevent oxidative stress. The name vtlA
(VIT1-like transporter) was proposed for iron homeostasis
related gene SCO2027.
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