ArticleExtremophiles : life under extreme conditions2017
Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.
Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Proteome-wide mapping of cysteine persulfidation in deep-sea hyperthermophilic archaea.Extremophiles : life under extreme conditions · 2026Article
- Regulation of gene expression under high hydrostatic pressure: the versatile role of the master regulator SurR in energy metabolism.Frontiers in microbiology · 2025Article
- NADPApplied and environmental microbiology · 2023Article
- Formate and hydrogen in hydrothermal vents and their use by extremely thermophilic methanogens and heterotrophs.Frontiers in microbiology · 2023Review
- TrmB Family Transcription Factor as a Thiol-Based Regulator of Oxidative Stress Response.mBio · 2022Article
- Identification of enriched hyperthermophilic microbial communities from a deep-sea hydrothermal vent chimney under electrolithoautotrophic culture conditions.Scientific reports · 2021Article
- Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020Review
- Direct Electron Transfer between theApplied and environmental microbiology · 2020Article
- Methionine Sulfoxide Reductases of Archaea.Antioxidants (Basel, Switzerland) · 2018Review
- Gene regulation of two ferredoxin:NADPExtremophiles : life under extreme conditions · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide oxidoreductases are redox enzymes that catalyze thiol-disulfide exchange reactions. These enzymes include thioredoxins, glutaredoxins, protein disulfide isomerases, disulfide bond formation A (DsbA) proteins, and Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO) homologues. In the genome of a hyperthermophilic archaeon, Thermococcus onnurineus NA1, the genes encoding one PfPDO homologue (TON_0319, Pdo) and three more thioredoxin- or glutaredoxin-like proteins (TON_0470, TON_0472, TON_0834) were identified. All except TON_0470 were recombinantly expressed and purified. Three purified proteins were reduced by a thioredoxin reductase (TrxR), indicating that each protein can form redox complex with TrxR. SurR, a transcription factor involved in the sulfur response, was tested for a protein target of a TrxR-redoxin system and only Pdo was identified to be capable of catalyzing the reduction of SurR. Electromobility shift assay demonstrated that SurR reduced by the TrxR-Pdo system could bind to the DNA probe with the SurR-binding motif, GTTttgAAC. In this study, we present the TrxR-Pdo couple as a redox-regulator for SurR in T. onnurineus NA1.
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