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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.

SUBMITTER: Wang T

PROVIDER: S-EPMC3532415 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Crystal structure of the human SUV39H1 chromodomain and its recognition of histone H3K9me2/3.

Wang Tao T Xu Chao C Liu Yanli Y Fan Kai K Li Zhihong Z Sun Xing X Ouyang Hui H Zhang Xuecheng X Zhang Jiahai J Li Yanjun Y Mackenzie Farrell F Min Jinrong J Tu Xiaoming X

PloS one 20121228 12

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, diffe ...[more]

PMID: 23285239

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