The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Phil Young | - |
dc.contributor.author | Bae, Kwang-Hee | - |
dc.contributor.author | Jeong, Dae Gwin | - |
dc.contributor.author | Chi, Seung-Wook | - |
dc.contributor.author | Moon, Jeong Hee | - |
dc.contributor.author | Kang, Seongman | - |
dc.contributor.author | Cho, Sayeon | - |
dc.contributor.author | Lee, Sang Chul | - |
dc.contributor.author | Park, Byoung Chul | - |
dc.contributor.author | Park, Sung Goo | - |
dc.date.accessioned | 2021-09-07T14:26:15Z | - |
dc.date.available | 2021-09-07T14:26:15Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2011-03 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/112898 | - |
dc.description.abstract | Glutathione peroxidases (Gpxs) are the key anti-oxidant enzymes found in Saccharomyces cerevisiae. Among the three Gpx isoforms, glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and modulates the activities of redox-sensitive thiol proteins involved in various biological reactions. By using a proteomic approach, glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH2; EC 1.2.1.12) was found as a candidate protein for interaction with Gpx3. GAPDH, a key enzyme in glycolysis, is a multi-functional protein with multiple intracellular localizations and diverse activities. To validate the interaction between Gpx3 and GAPDH2, immunoprecipitation and a pull-down assay were carried out. The results clearly showed that GAPDH2 interacts with Gpx3 through its carboxyl-terminal domain both in vitro and in vivo. Additionally, Gpx3 helps to reduce the S-nitrosylation of GAPDH upon nitric oxide (NO) stress; this subsequently increases cellular viability. On the basis of our findings, we suggest that Gpx3 protects GAPDH from NO stress and thereby contributes to the maintenance of homeostasis during exposure to NO stress. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | KOREAN SOC MOLECULAR & CELLULAR BIOLOGY | - |
dc.subject | OXIDATIVE STRESS | - |
dc.subject | GAPDH | - |
dc.title | The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kang, Seongman | - |
dc.identifier.doi | 10.1007/s10059-011-0029-3 | - |
dc.identifier.scopusid | 2-s2.0-79959976468 | - |
dc.identifier.wosid | 000288805400008 | - |
dc.identifier.bibliographicCitation | MOLECULES AND CELLS, v.31, no.3, pp.255 - 259 | - |
dc.relation.isPartOf | MOLECULES AND CELLS | - |
dc.citation.title | MOLECULES AND CELLS | - |
dc.citation.volume | 31 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 255 | - |
dc.citation.endPage | 259 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | OXIDATIVE STRESS | - |
dc.subject.keywordPlus | GAPDH | - |
dc.subject.keywordAuthor | Apoptosis | - |
dc.subject.keywordAuthor | GAPDH | - |
dc.subject.keywordAuthor | glutathione peroxidase 3 | - |
dc.subject.keywordAuthor | nitosylation | - |
dc.subject.keywordAuthor | NO stress | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.