3mts

Publication Abstract from PubMed

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.

Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3.,Wang T, Xu C, Liu Y, Fan K, Li Z, Sun X, Ouyang H, Zhang X, Zhang J, Li Y, Mackenzie F, Min J, Tu X PLoS One. 2012;7(12):e52977. doi: 10.1371/journal.pone.0052977. Epub 2012 Dec 28. PMID:23285239^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.