Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1

被引：144

作者：

Musselman, Catherine A. ^{[1
]}

Avvakumov, Nikita ^{[2
]}

Watanabe, Reiko ^{[3
]}

Abraham, Christopher G. ^{[4
]}

Lalonde, Marie-Eve ^{[2
]}

Hong, Zehui ^{[5
]}

Allen, Christopher ^{[6
]}

Roy, Siddhartha ^{[1
]}

Nunez, James K. ^{[1
]}

Nickoloff, Jac ^{[6
]}

Kulesza, Caroline A. ^{[4
]}

Yasui, Akira ^{[3
]}

Cote, Jacques ^{[2
]}

Kutateladze, Tatiana G. ^{[1
]}

机构：

[1] Univ Colorado, Sch Med, Dept Pharmacol, Aurora, CO USA

[2] Univ Laval, Canc Res Ctr, Hotel Dieu Quebec CHUQ, Quebec City, PQ, Canada

[3] Tohoku Univ, Inst Dev Aging & Canc, Div Dynam Proteome Canc & Aging, Aoba Ku, Sendai, Miyagi 980, Japan

[4] Univ Colorado, Sch Med, Dept Microbiol, Aurora, CO USA

[5] Southeast Univ, Sch Med, Dept Genet & Dev Biol, Nanjing, Jiangsu, Peoples R China

[6] Colorado State Univ, Dept Environm & Radiol Hlth Sci, Ft Collins, CO 80523 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 12期

基金：

美国国家卫生研究院; 加拿大健康研究院;

关键词：

HISTONE METHYLTRANSFERASE ACTIVITY; POLYCOMB GROUP PROTEIN; REPRESSIVE COMPLEX 2; STRUCTURAL BASIS; TARGET GENES; METHYLATION; H3; BINDING; PRC2; ENHANCER;

D O I：

10.1038/nsmb.2435

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：

The PHD finger protein 1 (PHF1) is essential in epigenetic regulation and genome maintenance. Here we show that the Tudor domain of human PHF1 binds to histone H3 trimethylated at Lys36 (H3K36me3). We report a 1.9-angstrom resolution crystal structure of the Tudor domain in complex with H3K36me3 and describe the molecular mechanism of H3K36me3 recognition using NMR. Binding of PHF1 to H3K36me3 inhibits the ability of the Polycomb PRC2 complex to methylate Lys27 of histone H3 in vitro and in vivo. Laser microirradiation data show that PHF1 is transiently recruited to DNA double-strand breaks, and PHF1 mutants impaired in the H3K36me3 interaction exhibit reduced retention at double-strand break sites. Together, our findings suggest that PHF1 can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response.

引用

页码：1266 / +

页数：9

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