ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression

Hong Wen (), Yuanyuan Li, Yuanxin Xi, Shiming Jiang, Sabrina Stratton, Danni Peng, Kaori Tanaka, Yongfeng Ren, Zheng Xia, Jun Wu, Bing Li, Michelle C. Barton, Wei Li (), Haitao Li () and Xiaobing Shi ()
Additional contact information
Hong Wen: The University of Texas MD Anderson Cancer Center
Yuanyuan Li: MOE Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University
Yuanxin Xi: Dan L. Duncan Cancer Center, Baylor College of Medicine
Shiming Jiang: The University of Texas MD Anderson Cancer Center
Sabrina Stratton: The University of Texas MD Anderson Cancer Center
Danni Peng: The University of Texas MD Anderson Cancer Center
Kaori Tanaka: The University of Texas MD Anderson Cancer Center
Yongfeng Ren: MOE Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University
Zheng Xia: Dan L. Duncan Cancer Center, Baylor College of Medicine
Jun Wu: The University of Texas Southwestern Medical Center
Bing Li: The University of Texas Southwestern Medical Center
Michelle C. Barton: The University of Texas MD Anderson Cancer Center
Wei Li: Dan L. Duncan Cancer Center, Baylor College of Medicine
Haitao Li: MOE Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University
Xiaobing Shi: The University of Texas MD Anderson Cancer Center

Nature, 2014, vol. 508, issue 7495, 263-268

Abstract: Candidate tumour suppressor ZMYND11 specifically recognizes histone K36 trimethylation on the histone variant H3.3 and helps regulate transcription elongation.

Date: 2014
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DOI: 10.1038/nature13045

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