Abstract
Recent research reveals that the YEATS domains preferentially recognize crotonylated lysines on histones. Here, we discuss the molecular mechanisms that enable this recognition and the biological significances of this interaction. The dynamics of histone crotonylation and its potential roles in the regulation of gene expression will also be discussed.
Keywords:
YEATS domain; aromatic-π stacking; histone crotonylation; reader; transcription.
MeSH terms
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Gene Expression Regulation, Fungal
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Histones / chemistry*
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Histones / metabolism*
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Models, Molecular
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Multigene Family
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
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Saccharomyces cerevisiae / chemistry
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / metabolism*
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Transcription, Genetic
Substances
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Histones
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Saccharomyces cerevisiae Proteins