Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

Alessandro Vezzoli; Nicolas Bonadies; Mark D Allen; Stefan M V Freund; Clara M Santiveri; Brynn T Kvinlaug; Brian J P Huntly; Berthold Göttgens; Mark Bycroft

doi:10.1038/nsmb.1797

Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

Alessandro Vezzoli, Nicolas Bonadies, Mark D Allen, Stefan M V Freund, Clara M Santiveri, Brynn T Kvinlaug, Brian J P Huntly, Berthold Göttgens, Mark Bycroft

University of Cambridge

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	617-619
Journal	Nature Structural Biology
Volume	17
Issue number	5
Early online date	18 Apr 2010
DOIs	https://doi.org/10.1038/nsmb.1797
Publication status	Published - 1 May 2010
Externally published	Yes

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title = "Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1",

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.",

author = "Alessandro Vezzoli and Nicolas Bonadies and Allen, {Mark D} and Freund, {Stefan M V} and Santiveri, {Clara M} and Kvinlaug, {Brynn T} and Huntly, {Brian J P} and Berthold G{\"o}ttgens and Mark Bycroft",

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T1 - Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

AU - Vezzoli, Alessandro

AU - Bonadies, Nicolas

AU - Allen, Mark D

AU - Freund, Stefan M V

AU - Santiveri, Clara M

AU - Kvinlaug, Brynn T

AU - Huntly, Brian J P

AU - Göttgens, Berthold

AU - Bycroft, Mark

PY - 2010/5/1

Y1 - 2010/5/1

N2 - 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.

AB - 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.

U2 - 10.1038/nsmb.1797

DO - 10.1038/nsmb.1797

M3 - Article

SN - 1545-9993

VL - 17

SP - 617

EP - 619

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 5

ER -

Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

Abstract

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