Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2

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• 作者：Hong Wu ; Alena Siarheyeva ; Hong Zeng ; Robert Lam ; Aiping Dong ; Xian-Hui Wu ; Yanjun Li ; Matthieu Schapira ; Masoud Vedadi ; Jinrong Min
• 关键词：Histone methyltransferase ; SET domain ; Crystal structure ; SUV420H1 ; SUV420H2
• 刊名：FEBS Letters
• 出版年：29 November, 2013
• 年：2013
• 卷：587
• 期：23
• 页码：3859-3868
• 全文大小：4292 K

文摘

SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. In this study, we present the high-resolution crystal structures of human SUV420H1 and SUV420H2 in complex with SAM, and report their substrate specificity. Both methyltransferases have a unique N-terminal domain and Zn-binding post-SET domain, and prefer the monomethylated histone H4K20 as a substrate in vitro. No histone H4K20 trimethylation activity was detected by our radioactivity-based assay for either enzyme, consistent with the presence of a conserved serine residue that forms a hydrogen bond with the target lysine side-chain and limits the methylation level.