Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner=효모 Gpx3의 글루타민 합성효소의 비효소적 분해의 억제

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dc.contributor.authorPhil Young Lee-
dc.contributor.authorC W Kho-
dc.contributor.authorDo Hee Lee-
dc.contributor.authorSunghyun Kang-
dc.contributor.authorS Kang-
dc.contributor.authorSang Chul Lee-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorS Cho-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:07:49Z-
dc.date.available2017-04-19T09:07:49Z-
dc.date.issued2007-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2007.08.035ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8036-
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+/O2 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.-
dc.publisherElsevier-
dc.titleGlutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner=효모 Gpx3의 글루타민 합성효소의 비효소적 분해의 억제-
dc.title.alternativeGlutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number2-
dc.citation.endPage409-
dc.citation.startPage405-
dc.citation.volume362-
dc.contributor.affiliatedAuthorPhil Young Lee-
dc.contributor.affiliatedAuthorDo Hee Lee-
dc.contributor.affiliatedAuthorSunghyun Kang-
dc.contributor.affiliatedAuthorSang Chul Lee-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName이필영-
dc.contributor.alternativeName고창원-
dc.contributor.alternativeName이도희-
dc.contributor.alternativeName강성현-
dc.contributor.alternativeName강성만-
dc.contributor.alternativeName이상철-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 362, no. 2, pp. 405-409-
dc.identifier.doi10.1016/j.bbrc.2007.08.035-
dc.subject.keywordGlutamine synthetase-
dc.subject.keywordGlutathione peroxidase 3-
dc.subject.keywordMFO system-
dc.subject.keywordOxidative stress-
dc.subject.keywordROS-
dc.subject.localGlutamine synthetase-
dc.subject.localGlutathione peroxidase 3-
dc.subject.localglutathione peroxidase 3-
dc.subject.localMFO system-
dc.subject.localOxidative stre-
dc.subject.localOxidative stress-
dc.subject.localOXIDATIVE STRESS-
dc.subject.localOxidative Stress-
dc.subject.localoxidative stress-
dc.subject.localReactive oxidative species-
dc.subject.localReactive oxygen species(ROS)-
dc.subject.localReactive oxygen species-
dc.subject.localReactive Oxygen Species (ROS)-
dc.subject.localReactive Oxygen Species-
dc.subject.localROS-
dc.subject.localReactive oxygen species (ROS)-
dc.subject.localreactive oxygen species-
dc.subject.localreactive oxygen species (ROS)-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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