Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1 SCIE SCOPUS

DC Field Value Language
dc.contributor.author Lim, Jae Kyu -
dc.contributor.author Jung, Hae-Chang -
dc.contributor.author Kang, Sung Gyun -
dc.contributor.author Lee, Hyun Sook -
dc.date.accessioned 2020-04-16T10:40:12Z -
dc.date.available 2020-04-16T10:40:12Z -
dc.date.created 2020-01-28 -
dc.date.issued 2017-05 -
dc.identifier.issn 1431-0651 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/1246 -
dc.description.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. -
dc.description.uri 1 -
dc.language English -
dc.publisher SPRINGER JAPAN KK -
dc.title Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1 -
dc.type Article -
dc.citation.endPage 498 -
dc.citation.startPage 491 -
dc.citation.title EXTREMOPHILES -
dc.citation.volume 21 -
dc.citation.number 3 -
dc.identifier.bibliographicCitation EXTREMOPHILES, v.21, no.3, pp.491 - 498 -
dc.identifier.doi 10.1007/s00792-017-0919-1 -
dc.identifier.scopusid 2-s2.0-85014091404 -
dc.identifier.wosid 000400233700006 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.description.isOpenAccess N -
dc.subject.keywordPlus ARCHAEON PYROCOCCUS-FURIOSUS -
dc.subject.keywordPlus GLUTAREDOXIN-LIKE PROTEIN -
dc.subject.keywordPlus BOND FORMATION -
dc.subject.keywordPlus SULFOLOBUS-SOLFATARICUS -
dc.subject.keywordPlus THIOREDOXIN REDUCTASE -
dc.subject.keywordPlus SACCHAROMYCES-CEREVISIAE -
dc.subject.keywordPlus TRANSCRIPTION FACTOR -
dc.subject.keywordPlus OXIDATIVE STRESS -
dc.subject.keywordPlus ELEMENTAL SULFUR -
dc.subject.keywordPlus IDENTIFICATION -
dc.subject.keywordAuthor Protein disulfide oxidoreductase -
dc.subject.keywordAuthor Thioredoxin reductase -
dc.subject.keywordAuthor SurR -
dc.subject.keywordAuthor Thermococcus onnurineus NA1 -
dc.subject.keywordAuthor Redox system -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology -
dc.relation.journalWebOfScienceCategory Microbiology -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Biochemistry & Molecular Biology -
dc.relation.journalResearchArea Microbiology -
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Marine Resources Research Division > Marine Biotechnology Research Center > 1. Journal Articles
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