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.
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页数：7
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