DC Field | Value | Language |
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dc.contributor.author | Park, MJ | - |
dc.contributor.author | Park, JH | - |
dc.contributor.author | Hahm, SH | - |
dc.contributor.author | Ko, SI | - |
dc.contributor.author | Lee, YR | - |
dc.contributor.author | Chung, JH | - |
dc.contributor.author | Sohn, SY | - |
dc.contributor.author | Cho, Y | - |
dc.contributor.author | Kang, LW | - |
dc.contributor.author | Han, YS | - |
dc.date.accessioned | 2016-04-01T03:04:15Z | - |
dc.date.available | 2016-04-01T03:04:15Z | - |
dc.date.created | 2010-04-28 | - |
dc.date.issued | 2009-10-02 | - |
dc.identifier.issn | 1568-7864 | - |
dc.identifier.other | 2009-OAK-0000020803 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/26213 | - |
dc.description.abstract | Rad9-Rad1-Hus1 (9-1-1) is a checkpoint protein complex playing roles in DNA damage sensing, cell cycle arrest, DNA repair or apoptosis. Human 8-oxoguanine DNA glycosylase (hOGG1) is the major DNA glycosylase responsible for repairing a specific aberrantly oxidized nucleotide, 7,8-dihydro-8-oxoguanine (8-oxoG). In this study, we identified a novel interaction between hOGG1 and human 9-1-1, and investigated the functional consequences of this interaction. Co-immunoprecipitation assays using transiently transfected HEK293 cells demonstrated an interaction between hOGG1 and the 9-1-1 proteins. Subsequently, GST pull-down assays using bacterially expressed and purified hOGG1-His and GST-fused 9-1-1 subunits (GST-hRad9, GST-hRad1, and GST-hHus1) demonstrated that hOGG1 interacted directly with the individual subunits of the human 9-1-1 complex. In vitro excision assay, which employed a DNA duplex containing an 8-oxoG/C mismatch, showed that hRad9, hRad1, and hHus1 enhanced the 8-oxoG excision and P-elimination activities of hOGG1. In addition, the presence of hRad9, hRad1, and hHus1 enhanced the formation of covalently cross-linked hOGG1-8-oxoG/C duplex complexes, as determined by a trapping assay using NaBH4. A trimeric human 9-1-1 complex was purified from Escherichia coli cell transformed with hRad9, His-fused hRad1, or His-fused hHus1 expressing vectors. It also showed the similar activity to enhance in vitro hOGG1 glycosylase activity, compared with individual human 9-1-1 subunits. Detection of 8-oxoG in HEK293 cells using flow cytometric and spectrofluorometric analysis revealed that over-expression of hOGG1 or human 9-1-1 reduced the formation of 8-oxoG residues following the H2O2 treatment. The highest 8-oxoG reduction was observed in HEK293 cells over-expressing hOGG1 and all the three subunits of human 9-1-1. These indicate that individual human 9-1-1 subunits and human 9-1-1 complex showed almost the same abilities to enhance the in vitro 8-oxoG excision activity of hOGG1, but that the greatest effect to remove 8-oxoG residues in H2O2-treated cells was derived from the 9-1-1 complex as a whole. (C) 2009 Elsevier B.V. All rights reserved. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.relation.isPartOf | DNA REPAIR | - |
dc.title | Repair activities of human 8-oxoguanine DNA glycosylase are stimulated by the interaction with human checkpoint sensor Rad9-Rad1-Hus1 complex | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1016/J.DNAREP.2009.06.004 | - |
dc.author.google | Park, MJ | - |
dc.author.google | Park, JH | - |
dc.author.google | Hahm, SH | - |
dc.author.google | Ko, SI | - |
dc.author.google | Lee, YR | - |
dc.author.google | Chung, JH | - |
dc.author.google | Sohn, SY | - |
dc.author.google | Cho, Y | - |
dc.author.google | Kang, LW | - |
dc.author.google | Han, YS | - |
dc.relation.volume | 8 | - |
dc.relation.issue | 10 | - |
dc.relation.startpage | 1190 | - |
dc.relation.lastpage | 1206 | - |
dc.contributor.id | 10082321 | - |
dc.relation.journal | DNA REPAIR | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | DNA REPAIR, v.8, no.10, pp.1190 - 1206 | - |
dc.identifier.wosid | 000271078300002 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 1206 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1190 | - |
dc.citation.title | DNA REPAIR | - |
dc.citation.volume | 8 | - |
dc.identifier.scopusid | 2-s2.0-70149088980 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 19 | - |
dc.description.scptc | 19 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | BASE EXCISION-REPAIR | - |
dc.subject.keywordPlus | HUMAN 3-METHYLADENINE-DNA GLYCOSYLASE | - |
dc.subject.keywordPlus | ENDONUCLEASE-III HNTH1 | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | N-GLYCOSYLASE | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | MISMATCH | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | HYPOXANTHINE | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordAuthor | Human 8-oxoguanine DNA glycosylase | - |
dc.subject.keywordAuthor | Human Rad9-Rad1-Hus1 (9-1-1) complex | - |
dc.subject.keywordAuthor | 8-Oxoguanine | - |
dc.subject.keywordAuthor | Excision activity | - |
dc.subject.keywordAuthor | Trapping assay | - |
dc.relation.journalWebOfScienceCategory | Genetics & Heredity | - |
dc.relation.journalWebOfScienceCategory | Toxicology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Genetics & Heredity | - |
dc.relation.journalResearchArea | Toxicology | - |
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