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Lee, Changwook
Structural Biology of Cellular Biochemistry Lab
Research Interests
  • Cell biology, structural biology, protein biochemistry, membrane biology, cancer biology


Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet

DC Field Value Language Kwon, Taewoo ko Chang, Jeong Ho ko Kwak, Eunyee ko Lee, Changwook ko Joachimiak, Andrzej ko Kim, Young Chang ko Lee, Jae Woon ko Cho, Yunje ko 2014-10-16T01:55:17Z - 2014-10-14 ko 2003-01 ko
dc.identifier.citation EMBO JOURNAL, v.22, no.2, pp.292 - 303 ko
dc.identifier.issn 0261-4189 ko
dc.identifier.uri -
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. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher OXFORD UNIV PRESS ko
dc.title Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0037439085 ko
dc.identifier.wosid 000180569900013 ko
dc.type.rims ART ko
dc.description.wostc 72 *
dc.description.scopustc 66 * 2015-05-06 * 2014-10-14 *
dc.identifier.doi 10.1093/emboj/cdg025 ko
dc.identifier.url ko
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