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Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3
Authors:Su Qin  Yahong Guo  Chao Xu  Chuanbing Bian  Minfei Fu  Sarah Gong  Jinrong Min
Affiliation:1. Structural Genomics Consortium, University of Toronto, 101 College St., Toronto, Ontario M5G 1L7, Canada;2. Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada;1. School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China;2. State Key Laboratory Breeding Base of Marine Genetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, Fujian, China;3. From the College of Life Sciences, Beijing Normal University, Beijing, 100875,;4. the National Institute of Biological Sciences, Beijing, 102206,;5. the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, and;6. the Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China;1. Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore;2. Cancer Science Institute of Singapore, Centre for Translational Medicine, Singapore 117599, Singapore;3. The State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Macau Special Administrative Region 999078, China;4. Cam-Su Genomic Resource Center, Soochow University, Suzhou 215123, China;5. Institute of Molecular and Cell Biology, Singapore 138673, Singapore;1. Biochemistry Department, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand;2. Research Infrastructure Centre, Division of Health Sciences, University of Otago, Dunedin 9054, New Zealand;1. Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan;2. Laboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan;3. Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan;4. Graduate School of Integrated Sciences for Life, Hiroshima University, 1-4-4 Kagamiyama, Higashi-Hiroshima 739-8258, Japan
Abstract:PRC2 is the major H3K27 methyltransferase and is responsible for maintaining repressed gene expression patterns throughout development. It contains four core components: EZH2, EED, SUZ12 and RbAp46/48 and some cell-type specific components. In this study, we focused on characterizing the histone binding domains of PHF1 and PHF19, and found that the Tudor domains of PHF1 and PHF19 selectively bind to histone H3K36me3. Structural analysis of these Tudor domains also shed light on how these Tudor domains selectively bind to histone H3K36me3. The histone H3K36me3 binding by the Tudor domains of PHF1, PHF19 and likely MTF2 provide another recruitment and regulatory mechanism for the PRC2 complex. In addition, we found that the first PHD domains of PHF1 and PHF19 do not exhibit histone H3K4 binding ability, nor do they affect the Tudor domain binding to histones.
Keywords:
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