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

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 th...

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Detalles Bibliográficos
Autores principales: Wang, Tao, Xu, Chao, Liu, Yanli, Fan, Kai, Li, Zhihong, Sun, Xing, Ouyang, Hui, Zhang, Xuecheng, Zhang, Jiahai, Li, Yanjun, MacKenzie, Farrell, Min, Jinrong, Tu, Xiaoming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3532415/
https://www.ncbi.nlm.nih.gov/pubmed/23285239
http://dx.doi.org/10.1371/journal.pone.0052977
Descripción
Sumario: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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