Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1
A Vezzoli, N Bonadies, MD Allen, SMV Freund… - Nature structural & …, 2010 - nature.com
Nature structural & molecular biology, 2010•nature.com
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.
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.
Abstract
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.
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