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A dimeric state for PRC2.

Chen Davidovich1, Karen J Goodrich1, Anne R Gooding1

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|July 5, 2014
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This summary is machine-generated.

Polycomb repressive complex-2 (PRC2) forms dimers that bind RNA. Multiple PRC2 dimers cooperatively bind a single RNA molecule, promoting epigenetic silencing.

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Area of Science:

  • Epigenetics and Gene Regulation
  • Molecular Biology
  • Chromatin Biology

Background:

  • Polycomb repressive complex-2 (PRC2) is a key histone methyltransferase.
  • PRC2 mediates epigenetic silencing essential for development and cancer.
  • Long non-coding RNAs (lncRNAs) are known to recruit PRC2 to chromatin.

Purpose of the Study:

  • To determine the stoichiometry of reconstituted human PRC2 complexes.
  • To investigate the interaction between PRC2 dimers and long non-coding RNAs (lncRNAs).
  • To elucidate the mechanism of PRC2 recruitment to chromatin mediated by lncRNAs.

Main Methods:

  • Analytical size exclusion chromatography (SEC).
  • SEC coupled with multi-angle light scattering (SEC-MALS).
  • Co-immunoprecipitation of differentially tagged PRC2 subunits.

Main Results:

  • Reconstituted human PRC2 exists as a dimer, confirmed by multiple biophysical techniques.
  • Each PRC2 dimer binds a single RNA molecule, despite containing multiple RNA-binding subunits.
  • Multiple PRC2 dimers exhibit cooperative binding to a single RNA molecule.

Conclusions:

  • PRC2 functions as a dimer in its interaction with RNA.
  • Cooperative binding of multiple PRC2 dimers to lncRNAs facilitates chromatin recruitment.
  • This mechanism suggests a model for nucleation of epigenetic repression by PRC2-RNA complexes.