DC Field | Value | Language |
---|---|---|
dc.contributor.author | Liu, Y | - |
dc.contributor.author | Sung, S | - |
dc.contributor.author | Kim, Y | - |
dc.contributor.author | Li, FY | - |
dc.contributor.author | Gwon, G | - |
dc.contributor.author | Jo, A | - |
dc.contributor.author | Kim, AK | - |
dc.contributor.author | Kim, T | - |
dc.contributor.author | Song, OK | - |
dc.contributor.author | Lee, SE | - |
dc.contributor.author | Cho, Y | - |
dc.date.accessioned | 2017-07-19T12:59:39Z | - |
dc.date.available | 2017-07-19T12:59:39Z | - |
dc.date.created | 2017-01-04 | - |
dc.date.issued | 2016-04-01 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/36742 | - |
dc.description.abstract | ATP-dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here, Methanococcus jannaschii MR-ATP gamma S-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATP gamma S-bound Rad50 nucleotide-binding domains. Duplex DNA cannot access the Mre11 active site in the ATP-free full-length MR complex. ATP hydrolysis drives rotation of the nucleotide-binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis-driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity. | - |
dc.language | English | - |
dc.publisher | Nature Publishing Group | - |
dc.relation.isPartOf | EMBO Journal | - |
dc.title | ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex | - |
dc.type | Article | - |
dc.identifier.doi | 10.15252/embj.201592462 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | EMBO Journal, v.35, no.7, pp.743 - 758 | - |
dc.identifier.wosid | 000373714300006 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 758 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 743 | - |
dc.citation.title | EMBO Journal | - |
dc.citation.volume | 35 | - |
dc.contributor.affiliatedAuthor | Cho, Y | - |
dc.identifier.scopusid | 2-s2.0-84952815466 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 20 | - |
dc.description.isOpenAccess | Y | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | STRAND BREAK REPAIR | - |
dc.subject.keywordPlus | MRE11 NUCLEASE | - |
dc.subject.keywordPlus | END RESECTION | - |
dc.subject.keywordPlus | CONFORMATIONAL-CHANGES | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | KINASE-ACTIVITY | - |
dc.subject.keywordPlus | RAD50 | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | RECOMBINATION | - |
dc.subject.keywordPlus | CHROMOSOME | - |
dc.subject.keywordAuthor | central groove | - |
dc.subject.keywordAuthor | DNA binding | - |
dc.subject.keywordAuthor | DNA melting | - |
dc.subject.keywordAuthor | Mre11/Rad50 | - |
dc.subject.keywordAuthor | nuclease | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
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