Article
Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription.
The Journal of biological chemistry - 20 Mar 2009
Li Bing, Jackson Jessica, Simon Matthew D, Fleharty Brian, Gogol Madelaine, Seidel Chris, Workman Jerry L, Shilatifard Ali
Abstract excerpt
Histone methylation is associated with both transcription activation and repression. However, the functions of different states of methylation remain largely elusive. Here, using methyl-lysine analog technology, we demonstrate that the histone deacetylase complex, Rpd3S, can distinguish the nucleosomes methylated to different extents and that K36me2 is sufficient to target Rpd3S in vitro. Through a genome-wide...
Topics
- Animals
- Genome, Human
- HeLa Cells
- Histone Deacetylase 2
- Histone Deacetylases
- Histone-Lysine N-Methyltransferase
- Histones
- Humans
- Lysine
- Methylation
