DC Field | Value | Language |
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dc.contributor.author | KIM, MIN SUNG | - |
dc.contributor.author | Chuenchor, Watchalee | - |
dc.contributor.author | Chen, Xuemin | - |
dc.contributor.author | Cui, Yanxiang | - |
dc.contributor.author | Zhang, Xing | - |
dc.contributor.author | Hong Zoud, Z | - |
dc.contributor.author | Gellert, Martin | - |
dc.contributor.author | Yang, Wei | - |
dc.date.accessioned | 2018-06-07T01:01:21Z | - |
dc.date.available | 2018-06-07T01:01:21Z | - |
dc.date.created | 2018-05-03 | - |
dc.date.issued | 2018-04 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/50102 | - |
dc.description.abstract | To initiate V(D) J recombination for generating the adaptive immune response of vertebrates, RAG1/2 recombinase cleaves DNA at a pair of recombination signal sequences, the 12- and 23-RSS. We have determined crystal and cryo-EM structures of RAG1/2 with DNA in the pre-reaction and hairpinforming complexes up to 2.75 angstrom resolution. Both protein and DNA exhibit structural plasticity and undergo dramatic conformational changes. Coding-flank DNAs extensively rotate, shift, and deform for nicking and hairpin formation. Two intertwined RAG1 subunits crisscross four times between the asymmetric pair of severely bent 12/23-RSS DNAs. Location-sensitive bending of 60 degrees and 150 degrees in 12- and 23-RSS spacers, respectively, must occur for RAG1/2 to capture the nonamers and pair the hep-tamers for symmetric double-strand breakage. DNA pairing is thus sequence-context dependent and structure specific, which partly explains the "beyond 12/23'' restriction. Finally, catalysis in crystallo reveals the process of DNA hairpin formation and its stabilization by interleaved base stacking. | - |
dc.language | English | - |
dc.publisher | Cell Press | - |
dc.relation.isPartOf | Molecular Cell | - |
dc.title | Cracking the DNA Code for V(D)J Recombination | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.molcel.2018.03.008 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Molecular Cell, v.70, no.2, pp.358 - 370 | - |
dc.identifier.wosid | 000430536000016 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 370 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 358 | - |
dc.citation.title | Molecular Cell | - |
dc.citation.volume | 70 | - |
dc.contributor.affiliatedAuthor | KIM, MIN SUNG | - |
dc.identifier.scopusid | 2-s2.0-85044610025 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 6 | - |
dc.description.isOpenAccess | Y | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | 12/23 RULE | - |
dc.subject.keywordPlus | 2 STEPS | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | CLEAVAGE | - |
dc.subject.keywordPlus | CRYOELECTRON MICROSCOPY | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | EM STRUCTURE DETERMINATION | - |
dc.subject.keywordPlus | RAG1 | - |
dc.subject.keywordPlus | SIGNAL SEQUENCE | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
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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