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Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner

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dc.contributor.authorLee, Phil Young-
dc.contributor.authorKho, Chang Won-
dc.contributor.authorLee, Do Hee-
dc.contributor.authorKang, Sunghyun-
dc.contributor.authorKang, Seongman-
dc.contributor.authorLee, Sang Chul-
dc.contributor.authorPark, Byoung Chul-
dc.contributor.authorCho, Sayeon-
dc.contributor.authorBae, Kwang-Hee-
dc.contributor.authorPark, Sung Goo-
dc.date.available2019-05-30T05:39:49Z-
dc.date.issued2007-10-
dc.identifier.issn0006-291X-
dc.identifier.issn1090-2104-
dc.identifier.urihttps://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23949-
dc.description.abstractGlutathione peroxidase 3 (Gpx3) is ubiquitously expressed and is important antioxidant enzyme in yeast. It modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathway and protein translocation. Through immunoprecipitation/two-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay, we found glutamine synthetase (GS; EC 6.3.1.2) as a candidate interacting protein with Gpx3. GS is a key enzyme in nitrogen metabolism and ammonium assimilation. It has been known that GS is non-enzymatically cleaved by ROS generated by MFO (thiol/ Fe3+/O-2 mixed-function oxidase) system. In this study, it is demonstrated that GS interacts with Gpx3 through its catalytic domain both in vivo and in vitro regardless of redox state. In addition, Gpx3 helps to protect GS from inactivation and degradation via oxidative stress in an activity-independent manner. Based on the results, it is suggested that Gpx3 protects GS from non-enzymatic proteolysis, thereby contributing to cell homeostasis when cell is exposed to oxidative stress. (c) 2007 Elsevier Inc. All rights reserved.-
dc.format.extent5-
dc.language영어-
dc.language.isoENG-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.titleGlutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner-
dc.typeArticle-
dc.identifier.doi10.1016/j.bbrc.2007.08.035-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.362, no.2, pp 405 - 409-
dc.description.isOpenAccessN-
dc.identifier.wosid000249464800031-
dc.identifier.scopusid2-s2.0-34548265133-
dc.citation.endPage409-
dc.citation.number2-
dc.citation.startPage405-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume362-
dc.type.docTypeArticle-
dc.publisher.location미국-
dc.subject.keywordAuthorglutathione peroxidase 3-
dc.subject.keywordAuthorglutamine synthetase-
dc.subject.keywordAuthorMFO system-
dc.subject.keywordAuthorROS-
dc.subject.keywordAuthoroxidative stress-
dc.subject.keywordPlusOXIDATIVE STRESS-
dc.subject.keywordPlusFREE-RADICALS-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusTHIOREDOXIN-
dc.subject.keywordPlusPEROXIDASE-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordPlusDAMAGE-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
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