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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Genome, Human / physiology
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HeLa Cells
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Histone Deacetylase 2
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Histone Deacetylases / genetics
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Histone Deacetylases / metabolism*
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Histone-Lysine N-Methyltransferase / genetics
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Histone-Lysine N-Methyltransferase / metabolism
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Histones / genetics
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Histones / metabolism*
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Humans
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Lysine / genetics
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Lysine / metabolism*
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Methylation
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Multienzyme Complexes / genetics
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Multienzyme Complexes / metabolism*
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Mutation
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Transcription, Genetic / physiology*
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Xenopus
Substances
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Histones
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Multienzyme Complexes
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Repressor Proteins
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Histone-Lysine N-Methyltransferase
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SETD2 protein, human
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Histone Deacetylase 2
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Histone Deacetylases
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Lysine