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Updated: Jan 16, 2026

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EPOP and MTF2 Activate PRC2 Activity through DNA-sequence specificity.

Jeffrey Granat1,2,3,4, Sanxiong Liu1,2,5,6,7,4, Luis Popoca1,2,8

  • 1Howard Hughes Medical Institute, NYU Langone Health, New York, NY 10016, USA.

Biorxiv : the Preprint Server for Biology
|October 3, 2025
PubMed
Summary
This summary is machine-generated.

The protein EPOP enhances Polycomb Repressive Complex 2 (PRC2) histone methyltransferase activity, aiding in H3K27me3 chromatin domain formation. EPOP cooperates with MTF2 and JARID2 for de novo H3K27me3 deposition.

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Area of Science:

  • Epigenetics
  • Chromatin Biology
  • Molecular Biology

Background:

  • Polycomb Repressive Complex 2 (PRC2) establishes facultative heterochromatin crucial for tissue-specific gene expression.
  • PRC2 catalyzes histone H3 lysine 27 tri-methylation (H3K27me3), a mark recognized by PRC1 for chromatin compaction.
  • Cofactors like MTF2 and JARID2 guide PRC2 to specific DNA-binding motifs, regulating its activity.

Purpose of the Study:

  • To investigate the role of EPOP in regulating PRC2 activity and chromatin localization.
  • To elucidate how EPOP influences PRC2's histone methyltransferase (HMT) function.
  • To understand EPOP's contribution to H3K27me3 deposition and chromatin domain formation.

Main Methods:

  • In vitro assays to measure PRC2 HMT activity with EPOP and MTF2.
  • In vivo EED-rescue system to assess PRC2 chromatin recruitment.
  • Dinucleosome binding assays to evaluate PRC2 chromatin-binding activity with EPOP and MTF2.

Main Results:

  • Both EPOP and MTF2 stimulate PRC2 HMT activity in vitro.
  • EPOP does not mediate PRC2 chromatin recruitment in vivo but promotes de novo H3K27me3 deposition with MTF2 and JARID2.
  • EPOP enhances PRC2 chromatin binding in a DNA-sequence dependent manner (GCN-rich), similar to MTF2 (GA-rich).

Conclusions:

  • EPOP functions as a PRC2-associated cofactor that enhances its HMT activity.
  • EPOP, MTF2, and JARID2 cooperate to promote H3K27me3 deposition at specific chromatin sites.
  • These cofactors collectively contribute to the formation of H3K27me3-chromatin domains through sequence-specific DNA interactions.