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Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2

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  • Sarah Cooper

    (Developmental Epigenetics, University of Oxford)

  • Anne Grijzenhout

    (Developmental Epigenetics, University of Oxford)

  • Elizabeth Underwood

    (Developmental Epigenetics, University of Oxford)

  • Katia Ancelin

    (Institut Curie, CNRS UMR3215, INSERM U934)

  • Tianyi Zhang

    (Developmental Epigenetics, University of Oxford)

  • Tatyana B. Nesterova

    (Developmental Epigenetics, University of Oxford)

  • Burcu Anil-Kirmizitas

    (Developmental Epigenetics, University of Oxford)

  • Andrew Bassett

    (Genome Engineering Oxford, Sir William Dunn School of Pathology, University of Oxford
    Present address: Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK)

  • Susanne M. Kooistra

    (Biotech Research and Innovation Centre (BRIC), University of Copenhagen
    Centre for Epigenetics, Ole Maaløes Vej 5, University of Copenhagen)

  • Karl Agger

    (Biotech Research and Innovation Centre (BRIC), University of Copenhagen
    Centre for Epigenetics, Ole Maaløes Vej 5, University of Copenhagen)

  • Kristian Helin

    (Biotech Research and Innovation Centre (BRIC), University of Copenhagen
    Centre for Epigenetics, Ole Maaløes Vej 5, University of Copenhagen
    The Danish Stem Cell Center (Danstem), University of Copenhagen)

  • Edith Heard

    (Institut Curie, CNRS UMR3215, INSERM U934)

  • Neil Brockdorff

    (Developmental Epigenetics, University of Oxford)

Abstract

The Polycomb repressive complexes PRC1 and PRC2 play a central role in developmental gene regulation in multicellular organisms. PRC1 and PRC2 modify chromatin by catalysing histone H2A lysine 119 ubiquitylation (H2AK119u1), and H3 lysine 27 methylation (H3K27me3), respectively. Reciprocal crosstalk between these modifications is critical for the formation of stable Polycomb domains at target gene loci. While the molecular mechanism for recognition of H3K27me3 by PRC1 is well defined, the interaction of PRC2 with H2AK119u1 is poorly understood. Here we demonstrate a critical role for the PRC2 cofactor Jarid2 in mediating the interaction of PRC2 with H2AK119u1. We identify a ubiquitin interaction motif at the amino-terminus of Jarid2, and demonstrate that this domain facilitates PRC2 localization to H2AK119u1 both in vivo and in vitro. Our findings ascribe a critical function to Jarid2 and define a key mechanism that links PRC1 and PRC2 in the establishment of Polycomb domains.

Suggested Citation

  • Sarah Cooper & Anne Grijzenhout & Elizabeth Underwood & Katia Ancelin & Tianyi Zhang & Tatyana B. Nesterova & Burcu Anil-Kirmizitas & Andrew Bassett & Susanne M. Kooistra & Karl Agger & Kristian Helin, 2016. "Jarid2 binds mono-ubiquitylated H2A lysine 119 to mediate crosstalk between Polycomb complexes PRC1 and PRC2," Nature Communications, Nature, vol. 7(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13661
    DOI: 10.1038/ncomms13661
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    Cited by:

    1. Andrew Keniry & Natasha Jansz & Linden J. Gearing & Iromi Wanigasuriya & Joseph Chen & Christian M. Nefzger & Peter F. Hickey & Quentin Gouil & Joy Liu & Kelsey A. Breslin & Megan Iminitoff & Tamara B, 2022. "BAF complex-mediated chromatin relaxation is required for establishment of X chromosome inactivation," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Chet H. Loh & Siebe Genesen & Matteo Perino & Magnus R. Bark & Gert Jan C. Veenstra, 2021. "Loss of PRC2 subunits primes lineage choice during exit of pluripotency," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    3. Lihu Gong & Xiuli Liu & Lianying Jiao & Xin Yang & Andrew Lemoff & Xin Liu, 2022. "CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    4. Xinyi Chen & Yiran Guo & Ting Zhao & Jiuwei Lu & Jian Fang & Yinsheng Wang & Gang Greg Wang & Jikui Song, 2024. "Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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