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Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. 总被引:14,自引:0,他引:14
H Wang R Cao L Xia H Erdjument-Bromage C Borchers P Tempst Y Zhang 《Molecular cell》2001,8(6):1207-1217
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PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin 总被引:10,自引:0,他引:10
Nishioka K Rice JC Sarma K Erdjument-Bromage H Werner J Wang Y Chuikov S Valenzuela P Tempst P Steward R Lis JT Allis CD Reinberg D 《Molecular cell》2002,9(6):1201-1213
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Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain 总被引:20,自引:0,他引:20
Feng Q Wang H Ng HH Erdjument-Bromage H Tempst P Struhl K Zhang Y 《Current biology : CB》2002,12(12):1052-1058
The N-terminal tails of core histones are subjected to multiple covalent modifications, including acetylation, methylation, and phosphorylation. Similar to acetylation, histone methylation has emerged as an important player in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Here, we report that lysine 79 (K79) of H3, located in the globular domain, can be methylated. K79 methylation occurs in a variety of organisms ranging from yeast to human. In budding yeast, K79 methylation is mediated by the silencing protein DOT1. Consistent with conservation of K79 methylation, DOT1 homologs can be found in a variety of eukaryotic organisms. We identified a human DOT1-like (DOT1L) protein and demonstrated that this protein possesses intrinsic H3-K79-specific histone methyltransferase (HMTase) activity in vitro and in vivo. Furthermore, we found that K79 methylation level is regulated throughout the cell cycle. Thus, our studies reveal a new methylation site and define a novel family of histone lysine methyltransferase. 相似文献
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Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage 总被引:36,自引:0,他引:36
Histone lysine methylation is a key regulator of gene expression and heterochromatin function, but little is known as to how this modification impinges on other chromatin activities. Here we demonstrate that a previously uncharacterized SET domain protein, Set9, is responsible for H4-K20 methylation in the fission yeast Schizosaccharomyces pombe. Surprisingly, H4-K20 methylation does not have any apparent role in the regulation of gene expression or heterochromatin function. Rather, we find the modification has a role in DNA damage response. Loss of Set9 activity or mutation of H4-K20 markedly impairs cell survival after genotoxic challenge and compromises the ability of cells to maintain checkpoint mediated cell cycle arrest. Genetic experiments link Set9 to Crb2, a homolog of the mammalian checkpoint protein 53BP1, and the enzyme is required for Crb2 localization to sites of DNA damage. These results argue that H4-K20 methylation functions as a "histone mark" required for the recruitment of the checkpoint protein Crb2. 相似文献
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Preferential dimethylation of histone H4 lysine 20 by Suv4-20 总被引:2,自引:0,他引:2
Yang H Pesavento JJ Starnes TW Cryderman DE Wallrath LL Kelleher NL Mizzen CA 《The Journal of biological chemistry》2008,283(18):12085-12092