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

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

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Title
Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
Author
Kwon, TaewooChang, Jeong HoKwak, EunyeeLee, ChangwookJoachimiak, AndrzejKim, Young ChangLee, Jae WoonCho, Yunje
Issue Date
2003-01
Publisher
OXFORD UNIV PRESS
Citation
EMBO JOURNAL, v.22, no.2, pp.292 - 303
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.
URI
https://scholarworks.unist.ac.kr/handle/201301/7286
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037439085
DOI
10.1093/emboj/cdg025
ISSN
0261-4189
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BIO_Journal Papers
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