title: The essential role of acetyllysine binding by the YEATS domain in transcriptional regulation.
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.
authors.affiliation: a Department of Pharmacology , University of Colorado School of Medicine , Aurora , CO , USA.
authors.forename: Forest H
authors.initials: FH
authors.lastname: Andrews
authors.affiliation: b Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.
authors.forename: Erin K
authors.initials: EK
authors.lastname: Shanle
authors.affiliation: b Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.
authors.forename: Brian D
authors.initials: BD
authors.lastname: Strahl
authors.affiliation: b Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.
authors.forename: Tatiana G
authors.initials: TG
authors.lastname: Kutateladze
mesh_terms: D000107:Acetylation; D001665:Binding Sites; D005786:Gene Expression Regulation; D011495:Histone-Lysine N-Methyltransferase; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D035362:Transcription Factor TFIID / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: C489901:MLLT3 protein, human; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; C090313:TAF14 protein, S cerevisiae; D035362:Transcription Factor TFIID; C473477:DOT1L protein, human; D008780:Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine
keywords: AF9; Taf14; YEATS domain; acetyllysine; transcription