Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes.
We describe distinct patterns of histone methylation during human cell cycle progression. Histone H4 methyltransferase activity was found to be cell cycle-regulated, consistent with increased H4 Lys 20 methylation at mitosis. This increase closely followed the cell cycle-regulated expression of the H4 Lys 20 methyltransferase, PR-Set7. Localization of PR-Set7 to mitotic chromosomes and subsequent increase in H4 Lys 20 methylation were inversely correlated to transient H4 Lys 16 acetylation in early S-phase. These data suggest that H4 Lys 20 methylation by PR-Set7 during mitosis acts to antagonize H4 Lys 16 acetylation and to establish a mechanism by which this mark is epigenetically transmitted.
Department of Biochemistry & Molecular Genetics, University of Virginia Health System, Charlottesville, Virginia 22908-0733, USA.
Judd C
JC
Rice
Kenichi
K
Nishioka
Kavitha
K
Sarma
Ruth
R
Steward
Danny
D
Reinberg
C David
CD
Allis
D000107:Acetylation; D002453:Cell Cycle / Q000502:physiology; D002875:Chromosomes / Q000201:enzymology; D006367:HeLa Cells; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000737:chemistry; D008745:Methylation; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism*; D008938:Mitosis / Q000502:physiology*; D011496:Protein Methyltransferases; D016196:S Phase / Q000502:physiology
D006657:Histones; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; C540312:SETD7 protein, human; D008239:Lysine