DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kwon, T | - |
dc.contributor.author | Chang, JH | - |
dc.contributor.author | Kwak, E | - |
dc.contributor.author | Lee, CW | - |
dc.contributor.author | Joachimiak, A | - |
dc.contributor.author | Kim, YC | - |
dc.contributor.author | Lee, JW | - |
dc.contributor.author | Cho, YJ | - |
dc.date.accessioned | 2016-03-31T13:59:55Z | - |
dc.date.available | 2016-03-31T13:59:55Z | - |
dc.date.created | 2009-03-05 | - |
dc.date.issued | 2003-01-15 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.other | 2003-OAK-0000010321 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/20960 | - |
dc.description.abstract | The methylation of lysine residues of histones plays a pivotal role in the regulation of chromatin structure and gene expression. Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 Angstrom resolution. The structures reveal an active site consisting of: (i) a binding pocket between the SET domain and a c-SET helix where an AdoMet molecule in an unusual conformation binds; (ii) a narrow substrate-specific channel that only unmethylated lysine residues can access; and (iii) a catalytic tyrosine residue. The methyl group of AdoMet is directed to the narrow channel where a substrate lysine enters from the opposite side. We demonstrate that SET7/9 can transfer two but not three methyl groups to unmodified Lys4 of H3 without substrate dissociation. The unusual features of the SET domain-containing HMTase discriminate between the un- and methylated lysine substrate, and the methylation sites for the histone H3 tail. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.relation.isPartOf | EMBO JOURNAL | - |
dc.title | Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1093/emboj/cdg025 | - |
dc.author.google | Kwon, T | - |
dc.author.google | Chang, JH | - |
dc.author.google | Kwak, E | - |
dc.author.google | Lee, CW | - |
dc.author.google | Joachimiak, A | - |
dc.author.google | Kim, YC | - |
dc.author.google | Lee, JW | - |
dc.author.google | Cho, YJ | - |
dc.relation.volume | 22 | - |
dc.relation.issue | 2 | - |
dc.relation.startpage | 292 | - |
dc.relation.lastpage | 303 | - |
dc.contributor.id | 10082321 | - |
dc.relation.journal | EMBO JOURNAL | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | EMBO JOURNAL, v.22, no.2, pp.292 - 303 | - |
dc.identifier.wosid | 000180569900013 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 303 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 292 | - |
dc.citation.title | EMBO JOURNAL | - |
dc.citation.volume | 22 | - |
dc.contributor.affiliatedAuthor | Cho, YJ | - |
dc.identifier.scopusid | 2-s2.0-0037439085 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 85 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | SET DOMAIN | - |
dc.subject.keywordPlus | COVALENT MODIFICATIONS | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | IN-VIVO | - |
dc.subject.keywordPlus | H3 | - |
dc.subject.keywordPlus | METHYLTRANSFERASE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | HETEROCHROMATIN | - |
dc.subject.keywordPlus | TRANSCRIPTION | - |
dc.subject.keywordPlus | SITE | - |
dc.subject.keywordAuthor | compact form of AdoMet | - |
dc.subject.keywordAuthor | 9 histone methyltransferase | - |
dc.subject.keywordAuthor | post-SET helix | - |
dc.subject.keywordAuthor | SET7 | - |
dc.subject.keywordAuthor | SET domain | - |
dc.subject.keywordAuthor | substrate-specific channel | - |
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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