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The role of Corynebacterium glutamicum spiA gene in whcA-mediated oxidative stress gene regulation

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dc.contributor.authorPark, Joon-Song-
dc.contributor.authorLee, Joo-Young-
dc.contributor.authorKim, Hyung-Joon-
dc.contributor.authorKim, Eung-Soo-
dc.contributor.authorKim, Pil-
dc.contributor.authorKim, Younhee-
dc.contributor.authorLee, Heung-Shick-
dc.date.accessioned2021-09-06T19:00:28Z-
dc.date.available2021-09-06T19:00:28Z-
dc.date.created2021-06-18-
dc.date.issued2012-06-
dc.identifier.issn0378-1097-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/108207-
dc.description.abstractThe Corynebacterium glutamicum WhcA protein, which inhibits the expression of oxidative stress response genes, is known to interact with the SpiA protein. In this study, we constructed and analyzed spiA mutant cells with the goal of better understanding the function of the spiA gene. A C. glutamicum strain overexpressing the spiA gene showed retarded cell growth, which was caused by an increased sensitivity to oxidants. Expression of the spiA and whcA genes was repressed by oxidant diamide, indicating coordinate regulation and dispensability of the genes in cells under oxidative stress. In the spiA-overexpressing cells, the trx gene, which encodes thioredoxin reductase, was severely repressed. Deletion of whcA in spiA-overexpressing cells (or vice versa) produced phenotypes similar to the wild-type strain. Collectively, these data demonstrate a negative regulatory role of the spiA gene in whcA-mediated oxidative stress response and provide additional clues on the mechanism by which the whcA gene is regulated.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherOXFORD UNIV PRESS-
dc.subjectPROTEIN-
dc.subjectEXPRESSION-
dc.subjectINTERACTS-
dc.subjectSURVIVAL-
dc.subjectBIOLOGY-
dc.subjectWHIB1-
dc.subjectHOST-
dc.titleThe role of Corynebacterium glutamicum spiA gene in whcA-mediated oxidative stress gene regulation-
dc.typeArticle-
dc.contributor.affiliatedAuthorLee, Heung-Shick-
dc.identifier.doi10.1111/j.1574-6968.2012.02554.x-
dc.identifier.scopusid2-s2.0-84860428036-
dc.identifier.wosid000303438800009-
dc.identifier.bibliographicCitationFEMS MICROBIOLOGY LETTERS, v.331, no.1, pp.63 - 69-
dc.relation.isPartOfFEMS MICROBIOLOGY LETTERS-
dc.citation.titleFEMS MICROBIOLOGY LETTERS-
dc.citation.volume331-
dc.citation.number1-
dc.citation.startPage63-
dc.citation.endPage69-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaMicrobiology-
dc.relation.journalWebOfScienceCategoryMicrobiology-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusINTERACTS-
dc.subject.keywordPlusSURVIVAL-
dc.subject.keywordPlusBIOLOGY-
dc.subject.keywordPlusWHIB1-
dc.subject.keywordPlusHOST-
dc.subject.keywordAuthorCorynebacterium glutamicum-
dc.subject.keywordAuthorwhcA-
dc.subject.keywordAuthorspiA-
dc.subject.keywordAuthoroxidative stress-
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