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DC Field | Value | Language |
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dc.citation.endPage | 303 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 292 | - |
dc.citation.title | EMBO JOURNAL | - |
dc.citation.volume | 22 | - |
dc.contributor.author | Kwon, Taewoo | - |
dc.contributor.author | Chang, Jeong Ho | - |
dc.contributor.author | Kwak, Eunyee | - |
dc.contributor.author | Lee, Changwook | - |
dc.contributor.author | Joachimiak, Andrzej | - |
dc.contributor.author | Kim, Young Chang | - |
dc.contributor.author | Lee, Jae Woon | - |
dc.contributor.author | Cho, Yunje | - |
dc.date.accessioned | 2023-12-22T11:36:09Z | - |
dc.date.available | 2023-12-22T11:36:09Z | - |
dc.date.created | 2014-10-14 | - |
dc.date.issued | 2003-01 | - |
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 A 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.identifier.bibliographicCitation | EMBO JOURNAL, v.22, no.2, pp.292 - 303 | - |
dc.identifier.doi | 10.1093/emboj/cdg025 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.scopusid | 2-s2.0-0037439085 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/7286 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037439085 | - |
dc.identifier.wosid | 000180569900013 | - |
dc.language | 영어 | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.title | Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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