Article open access publication

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

Nature Communications, Springer Nature, ISSN 2041-1723

Volume 7, 1, 2016

DOI:10.1038/ncomms13661, Dimensions: pub.1041825071, PMC: PMC5133711, PMID: 27892467,

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  1. (1) University of Oxford, grid.4991.5
  2. (2) Institut Curie, CNRS UMR3215, INSERM U934, 26 rue d'Ulm, 75248, Paris, France
  3. (3) Present address: Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK
  4. (4) University of Copenhagen, grid.5254.6, KU

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Denmark

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Description

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.

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University of Copenhagen

Danish Open Access Indicator

2016: Realized

Research area: Science & Technology

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2016: Level 2

Research area: Science & Technology

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Times Cited: 91

Field Citation Ratio (FCR): 14.6

Relative Citation ratio (RCR): 3.15

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