Histone H4 acetylation differentially modulates arginine methylation by an in Cis mechanism.

ABSTRACT: Histone H4 undergoes extensive post-translational modifications (PTMs) at its N-terminal tail. Many of these PTMs profoundly affect the on and off status of gene transcription. The molecular mechanism by which histone PTMs modulate genetic and epigenetic processes is not fully understood. In particular, how a PTM mark affects the presence and level of other histone modification marks needs to be addressed and is essential for better understanding the molecular basis of histone code hypothesis. To dissect the interplaying relationship between different histone modification marks, we investigated how individual lysine acetylations and their different combinations at the H4 tail affect Arg-3 methylation in cis. Our data reveal that the effect of lysine acetylation on arginine methylation depe

SUBMITTER: Feng Y 

PROVIDER: S-EPMC3121530 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature