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2 results on '"Suv420h2"'

1. Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.

Author

Wu, Hong, Siarheyeva, Alena, Zeng, Hong, Lam, Robert, Dong, Aiping, Wu, Xian-Hui, Li, Yanjun, Schapira, Matthieu, Vedadi, Masoud, and Min, Jinrong

Subjects
*CRYSTAL structure, *HISTONE methyltransferases, *N-terminal residues, *ZINC transporters, *BIOLOGICAL assay
Abstract

Highlights: [•] We report the first crystal structures of SUV420H1 and SUV420H2. [•] SUV420H1 and SUV420H2 exhibit unique N-terminal and Zn-binding post-SET domains. [•] We developed the first in vitro assay for characterizing and screening SUV420H1 and SUV420H2 in a 384-well format. [Copyright &y& Elsevier]

Published
2013
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2. Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2

Author

Yanjun Li, Jinrong Min, Aiping Dong, Alena Siarheyeva, Matthieu Schapira, Masoud Vedadi, Robert Lam, Hong Zeng, Hong Wu, and Xian-Hui Wu

Subjects
S-Adenosylmethionine, Methyltransferase, Molecular Sequence Data, Biophysics, Biology, Crystallography, X-Ray, Methylation, Biochemistry, Substrate Specificity, Histones, Histone H4, 03 medical and health sciences, 0302 clinical medicine, Histone H1, Structural Biology, Histone H2A, Histone methylation, Genetics, Humans, Histone code, Amino Acid Sequence, Histone octamer, Molecular Biology, 030304 developmental biology, 0303 health sciences, Binding Sites, Crystal structure, SUV420H2, SUV420H1, Histone-Lysine N-Methyltransferase, Cell Biology, Molecular Docking Simulation, SET domain, Zinc, Histone methyltransferase, 030220 oncology & carcinogenesis, Mutation
Abstract

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.

Published
2013

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