Functional Landscape of PCGF Proteins Reveals Both RING1A/B-Dependent-and RING1A/B-Independent-Specific Activities

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Polycomb repressive complexes 1 and 2 (PRC1 and PRC2) control cell identity by establishing facultative heterochromatin repressive domains at common sets of target genes. PRC1, which deposits H2Aub1 through the E3 ligases RING1A/B, forms six biochemically distinct subcomplexes depending on the assembled PCGF protein (PCGF1–PCGF6); however, it is yet unclear whether these subcomplexes have also specific activities. Here we show that PCGF1 and PCGF2 largely compensate for each other, while other PCGF proteins have high levels of specificity for distinct target genes. PCGF2 associates with transcription repression, whereas PCGF3 and PCGF6 associate with actively transcribed genes. Notably, PCGF3 and PCGF6 complexes can assemble and be recruited to several active sites independently of RING1A/B activity (therefore, of PRC1). For chromatin recruitment, the PCGF6 complex requires the combinatorial activities of its MGA-MAX and E2F6-DP1 subunits, while PCGF3 requires an interaction with the USF1 DNA binding transcription factor. PRC1 encompasses different sub-complexes with distinct biochemical properties. Scelfo et al. dissect these activities, highlighting their little redundancy and high functional specificity. PRC1 sub-complexes associate specifically with transcriptional repression or activation, can function independently of the core RING1A/B enzymes, and can be recruited to chromatin by specific DNA binding activities.

Original languageEnglish
Pages (from-to)1037-1052.e7
JournalMolecular Cell
Issue number5
Publication statusPublished - Jun 6 2019


  • EZH2
  • H2A ubiquitination
  • H3K27me3
  • MGA
  • MYC
  • PCGF
  • Polycomb
  • PRC1
  • RING1B
  • USF1

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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