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

被引：168

作者：

Vezzoli, Alessandro ^{[1
]}

Bonadies, Nicolas ^{[2
]}

Allen, Mark D. ^{[1
]}

Freund, Stefan M. V. ^{[3
]}

Santiveri, Clara M. ^{[1
]}

Kvinlaug, Brynn T. ^{[2
]}

Huntly, Brian J. P. ^{[2
]}

Goettgens, Berthold ^{[2
]}

Bycroft, Mark ^{[1
]}

机构：

[1] MRC, Ctr Prot Engn, Cambridge, England

[2] Univ Cambridge, Cambridge Inst Med Res, Dept Haematol, Cambridge, England

[3] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2010年 / 17卷 / 05期

基金：

英国医学研究理事会;

关键词：

BINDING MODULES; STEM-CELLS; CHROMATIN; PROTEIN; METHYLATION; FAMILY;

D O I：

10.1038/nsmb.1797

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：617 / 619

页数：3

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