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RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3 |
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| Authors: | Tavares Lígia Dimitrova Emilia Oxley David Webster Judith Poot Raymond Demmers Jeroen Bezstarosti Karel Taylor Stephen Ura Hiroki Koide Hiroshi Wutz Anton Vidal Miguel Elderkin Sarah Brockdorff Neil |
| Affiliation: | 1 Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK 2 Nuclear Dynamics, Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK 3 Mass Spectrometry, Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK 4 Department of Cell Biology, Erasmus Medical Center, Dr. Molewaterplein 50, 3015GE Rotterdam, The Netherlands 5 Proteomics Center, Erasmus Medical Center, Dr. Molewaterplein 50, 3015GE Rotterdam, The Netherlands 6 Computational Biology Research Group, WIMM, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK 7 Department of Stem Cell Biology, Graduate School of Medical Science, Kanazawa University, 13-1 Takaramachi, Kanazawa, Ishikawa 920-8640, Japan 8 Wellcome Trust Centre for Stem Cell Research, Tennis Court Road, Cambridge CB2 1QR, UK 9 Cell Proliferation and Development, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Cientificas (CSIC), 28040 Madrid, Spain |
| Abstract: | Polycomb-repressive complex 1 (PRC1) has a central role in the regulation of heritable gene silencing during differentiation and development. PRC1 recruitment is generally attributed to interaction of the chromodomain of the core protein Polycomb with trimethyl histone H3K27 (H3K27me3), catalyzed by a second complex, PRC2. Unexpectedly we find that RING1B, the catalytic subunit of PRC1, and associated monoubiquitylation of histone H2A are targeted to closely overlapping sites in wild-type and PRC2-deficient mouse embryonic stem cells (mESCs), demonstrating an H3K27me3-independent pathway for recruitment of PRC1 activity. We show that this pathway is mediated by RYBP-PRC1, a complex comprising catalytic subunits of PRC1 and the protein RYBP. RYBP-PRC1 is recruited to target loci in mESCs and is also involved in Xist RNA-mediated silencing, the latter suggesting a wider role in Polycomb silencing. We discuss the implications of these findings for understanding recruitment and function of Polycomb repressors. |
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