title: The Taf14 YEATS domain is a reader of histone crotonylation.
abstract: The discovery of new histone modifications is unfolding at startling rates; however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation, an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine-binding activity.
authors.affiliation: Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA.
authors.forename: Forest H
authors.initials: FH
authors.lastname: Andrews
authors.affiliation: Department of Biochemistry &Biophysics, the University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA.
authors.forename: Stephen A
authors.initials: SA
authors.lastname: Shinsky
authors.affiliation: Department of Biochemistry &Biophysics, the University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA.
authors.forename: Erin K
authors.initials: EK
authors.lastname: Shanle
authors.affiliation: Department of Biochemistry &Biophysics, the University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA.
authors.forename: Joseph B
authors.initials: JB
authors.lastname: Bridgers
authors.affiliation: Department of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
authors.forename: Anneliese
authors.initials: A
authors.lastname: Gest
authors.affiliation: Department of Biochemistry &Biophysics, the University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA.
authors.forename: Ian K
authors.initials: IK
authors.lastname: Tsun
authors.affiliation: Department of Biochemistry &Biophysics, the University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA.
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Krajewski
authors.affiliation: Department of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
authors.forename: Xiaobing
authors.identifier: 0000-0001-5242-8189
authors.initials: X
authors.lastname: Shi
authors.affiliation: Department of Biochemistry &Biophysics, the University of North Carolina School of Medicine, Chapel Hill, North Carolina, USA.
authors.forename: Brian D
authors.initials: BD
authors.lastname: Strahl
authors.affiliation: Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA.
authors.forename: Tatiana G
authors.initials: TG
authors.lastname: Kutateladze
mesh_terms: D044127:Epigenesis, Genetic; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D000072417:Protein Domains; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D035362:Transcription Factor TFIID / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; C090313:TAF14 protein, S cerevisiae; D035362:Transcription Factor TFIID; D008239:Lysine