Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3

被引：60

作者：

Wang, Tao ^{[3
]}

Xu, Chao ^{[1
,2
]}

Liu, Yanli ^{[1
,2
,4
]}

Fan, Kai ^{[3
]}

Li, Zhihong ^{[1
,2
]}

Sun, Xing ^{[1
,2
]}

Ouyang, Hui ^{[1
,2
]}

Zhang, Xuecheng ^{[5
]}

Zhang, Jiahai ^{[3
]}

Li, Yanjun ^{[1
,2
]}

MacKenzie, Farrell ^{[1
,2
]}

Min, Jinrong ^{[1
,2
,4
]}

Tu, Xiaoming ^{[3
]}

机构：

[1] Univ Toronto, Struct Genom Consortium, Toronto, ON, Canada

[2] Univ Toronto, Dept Physiol, Toronto, ON, Canada

[3] Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China

[4] Huazhong Normal Univ, Coll Life Sci, Hubei Key Lab Genet Regulat & Integrat Biol, Wuhan, Peoples R China

[5] Anhui Univ, Sch Life Sci, Hefei 230039, Anhui, Peoples R China

来源：

PLOS ONE | 2012年 / 7卷 / 12期

基金：

英国惠康基金;

关键词：

METHYLTRANSFERASE SUV39H1; H3; COMPLEX; BINDING; METHYLATION; SPECIFICITY; PROTEINS; RECRUITMENT; REFINEMENT; MARKS;

D O I：

10.1371/journal.pone.0052977

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页数：7

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