Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription.
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.
Li
Bing
B
Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
Jackson
Jessica
J
Simon
Matthew D
MD
Fleharty
Brian
B
Gogol
Madelaine
M
Seidel
Chris
C
Workman
Jerry L
JL
Shilatifard
Ali
A
D000818:Animals; D015894:Genome, Human / Q000502:physiology; D006367:HeLa Cells; D056464:Histone Deacetylase 2; D006655:Histone Deacetylases / Q000235:genetics / Q000378:metabolism*; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic / Q000502:physiology*; D014981:Xenopus
D006657:Histones; D009097:Multienzyme Complexes; D012097:Repressor Proteins; D011495:Histone-Lysine N-Methyltransferase; C521636:SETD2 protein, human; D056464:Histone Deacetylase 2; D006655:Histone Deacetylases; D008239:Lysine