Abstract
The presence of histone H3 lysine 36 methylation (H3K36me) correlates with actively transcribed genes. In yeast, histone H3K36me mediated by KMT3 (also known as Set2) recruits a histone deacetylase complex, Rpd3s, to ensure the fidelity of transcription initiation. We report the purification of human KMT3a (also known as HYPB or hSet2) complex and the identification of a novel, higher eukaryotic specific subunit, heterogeneous nuclear ribonucleoprotein L (HnRNP-L). Interestingly, although KMT3a has intrinsic activity in vitro, HnRNP-L is essential in vivo. Moreover, KMT3a generates mono-, di-, and trimethylated products in vitro, but RNA interference against KMT3a or HnRNP-L down-regulates exclusively the H3K36me3 mark in vivo.
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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Cell Line
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Heterogeneous-Nuclear Ribonucleoprotein L / chemistry*
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Heterogeneous-Nuclear Ribonucleoprotein L / metabolism*
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Histone-Lysine N-Methyltransferase / metabolism*
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Histones / metabolism
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Humans
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Kidney / embryology
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Lysine / metabolism
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Methylation
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Methyltransferases / chemistry
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Methyltransferases / isolation & purification
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Methyltransferases / metabolism*
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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Protein Subunits / chemistry
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Protein Subunits / metabolism
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Ribonucleases
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Transfection
Substances
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Heterogeneous-Nuclear Ribonucleoprotein L
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Histones
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Peptide Fragments
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Protein Subunits
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Methyltransferases
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Histone-Lysine N-Methyltransferase
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SETD2 protein, human
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Ribonucleases
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Lysine