title: Crystal structure of the human SUV39H1 chromodomain and its recognition of histone H3K9me2/3.
abstract: SUV39H1, the first identified histone lysine methyltransferase in human, is involved in chromatin modification and gene regulation. SUV39H1 contains a chromodomain in its N-terminus, which potentially plays a role in methyl-lysine recognition and SUV39H1 targeting. In this study, the structure of the chromodomain of human SUV39H1 was determined by X-ray crystallography. The SUV39H1 chromodomain displays a generally conserved structure fold compared with other solved chromodomains. However, different from other chromodomains, the SUV39H1 chromodomain possesses a much longer helix at its C-terminus. Furthermore, the SUV39H1 chromodomain was shown to recognize histone H3K9me2/3 specifically.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Science, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
authors.forename: Tao
authors.initials: T
authors.lastname: Wang
authors.forename: Chao
authors.initials: C
authors.lastname: Xu
authors.forename: Yanli
authors.initials: Y
authors.lastname: Liu
authors.forename: Kai
authors.initials: K
authors.lastname: Fan
authors.forename: Zhihong
authors.initials: Z
authors.lastname: Li
authors.forename: Xing
authors.initials: X
authors.lastname: Sun
authors.forename: Hui
authors.initials: H
authors.lastname: Ouyang
authors.forename: Xuecheng
authors.initials: X
authors.lastname: Zhang
authors.forename: Jiahai
authors.initials: J
authors.lastname: Zhang
authors.forename: Yanjun
authors.initials: Y
authors.lastname: Li
authors.forename: Farrell
authors.initials: F
authors.lastname: Mackenzie
authors.forename: Jinrong
authors.initials: J
authors.lastname: Min
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Tu
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000737:chemistry / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000502:physiology; D054730:Protein Interaction Domains and Motifs / Q000502:physiology; D060066:Protein Interaction Maps; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
chemical_list: D006657:Histones; D012097:Repressor Proteins; C407843:SUV39H1 protein, human; D008780:Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine