Polycomb-like proteins link the PRC2 complex to CpG islands

Haojie Li, Robert Liefke, Junyi Jiang, Jesse Vigoda Kurland, Wei Tian, Pujuan Deng, Weidi Zhang, Qian He, Dinshaw J. Patel, Martha L. Bulyk, Yang Shi and Zhanxin Wang ()
Additional contact information
Haojie Li: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University
Robert Liefke: Boston Children’s Hospital
Junyi Jiang: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University
Jesse Vigoda Kurland: Brigham and Women’s Hospital and Harvard Medical School
Wei Tian: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University
Pujuan Deng: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University
Weidi Zhang: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University
Qian He: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University
Dinshaw J. Patel: Structural Biology Program, Memorial Sloan-Kettering Cancer Center
Martha L. Bulyk: Brigham and Women’s Hospital and Harvard Medical School
Yang Shi: Boston Children’s Hospital
Zhanxin Wang: Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University

Nature, 2017, vol. 549, issue 7671, 287-291

Abstract: Crystal structures of the Polycomb-like proteins PHF1 and MTF2 with bound DNA and histone peptides show that extended homologous regions of the two proteins form a winged-helix structure that has an unexpected mechanism of binding to unmethylated CpG-containing DNA motifs.

Date: 2017
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DOI: 10.1038/nature23881

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