Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1.
Trimethylation of Lys36 in histone H3 (H3K36me3) coordinates events associated with the elongation phase of transcription and is also emerging as an important epigenetic regulator of cell growth and differentiation. We have identified the PWWP domain of bromo and plant homeodomain (PHD) finger-containing protein 1 (BRPF1) as a H3K36me3 binding module and have determined the structure of this domain in complex with an H3K36me3-derived peptide.
Vezzoli
Alessandro
A
MRC Centre for Protein Engineering, Cambridge, UK.
Bonadies
Nicolas
N
Allen
Mark D
MD
Freund
Stefan M V
SM
Santiveri
Clara M
CM
Kvinlaug
Brynn T
BT
Huntly
Brian J P
BJ
Göttgens
Berthold
B
Bycroft
Mark
M
D048868:Adaptor Proteins, Signal Transducing; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D000092468:Bromodomain Containing Proteins
D048868:Adaptor Proteins, Signal Transducing; D004268:DNA-Binding Proteins; D006657:Histones; D009687:Nuclear Proteins; C086011:BRPF1 protein, human; D000092468:Bromodomain Containing Proteins
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