Abstract
The YEATS domains of AF9 and Taf14 have recently been found to recognize the histone H3K9ac modification. In this commentary, we discuss the mechanistic and biological implications of this interaction. We compare structures of the YEATS-H3K9ac complexes the highlighting a novel mechanism for the acetyllysine recognition through the aromatic cage. We also summarize the latest findings underscoring a critical role of the acetyllysine binding function of AF9 and Taf14 in transcriptional regulation and DNA repair.
Keywords:
AF9; Taf14; YEATS domain; acetyllysine; transcription.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Acetylation
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Binding Sites
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Gene Expression Regulation
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Histone-Lysine N-Methyltransferase
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Humans
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Lysine / metabolism*
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Methyltransferases / genetics
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Methyltransferases / metabolism
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Protein Conformation
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Protein Structure, Tertiary
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Transcription Factor TFIID / chemistry*
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Transcription Factor TFIID / genetics
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Transcription Factor TFIID / metabolism*
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Transcription, Genetic
Substances
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MLLT3 protein, human
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Nuclear Proteins
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Saccharomyces cerevisiae Proteins
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TAF14 protein, S cerevisiae
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Transcription Factor TFIID
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DOT1L protein, human
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Methyltransferases
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Histone-Lysine N-Methyltransferase
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Lysine