Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response.
The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. Our findings establish a highly conserved acetyllysine reader function for the YEATS domain protein family and highlight the significance of this interaction for Taf14.
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Erin K
EK
Shanle
Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA;
Forest H
FH
Andrews
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Hashem
H
Meriesh
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA; Curriculum in Genetics and Molecular Biology, The University of North Carolina at Chapel Hill, North Carolina 27599 USA;
Stephen L
SL
McDaniel
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Raghuvar
R
Dronamraju
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA; Curriculum in Genetics and Molecular Biology, The University of North Carolina at Chapel Hill, North Carolina 27599 USA;
Julia V
JV
DiFiore
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Deepak
D
Jha
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA; Curriculum in Genetics and Molecular Biology, The University of North Carolina at Chapel Hill, North Carolina 27599 USA;
Glenn G
GG
Wozniak
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Joseph B
JB
Bridgers
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Jenny L
JL
Kerschner
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Krzysztof
K
Krajewski
Department of Biology, Stanford University, Stanford, California 94305 USA.
Glòria Mas
GM
Martín
Department of Biology, Stanford University, Stanford, California 94305 USA.
Ashby J
AJ
Morrison
Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA;
Tatiana G
TG
Kutateladze
Department of Biochemistry and Biophysics, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA; Curriculum in Genetics and Molecular Biology, The University of North Carolina at Chapel Hill, North Carolina 27599 USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599 USA;
Brian D
BD
Strahl
D000107:Acetylation; D004249:DNA Damage; D004260:DNA Repair / Q000235:genetics*; D015966:Gene Expression Regulation, Fungal / Q000235:genetics*; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D035362:Transcription Factor TFIID / Q000378:metabolism*
D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; C090313:TAF14 protein, S cerevisiae; D035362:Transcription Factor TFIID
DNA damage; Taf14; YEATS domain; gene transcription; histone acetylation