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J Biol Chem. 2009 Mar 20;284(12):7970-6. doi: 10.1074/jbc.M808220200. Epub 2009 Jan 20.

Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription.

Author information

1
Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.

Abstract

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 survey, we identified a few mutants in which the level of K36me3 is significantly reduced, whereas the level of K36me2 is sustained. Transcription analysis and genome-wide histone modification studies on these mutants suggested that K36me2 is sufficient to target Rpd3S in vivo, thereby maintaining a functional Set2-Rpd3S pathway.

PMID:
19155214
PMCID:
PMC2658090
DOI:
10.1074/jbc.M808220200
[Indexed for MEDLINE]
Free PMC Article

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