Article

 

A dimeric state for PRC2. Public Deposited

https://scholar.colorado.edu/concern/articles/7p88ch29h
Abstract
  • Polycomb repressive complex-2 (PRC2) is a histone methyltransferase required for epigenetic silencing during development and cancer. Long non-coding RNAs (lncRNAs) can recruit PRC2 to chromatin. Previous studies identified PRC2 subunits in a complex with the apparent molecular weight of a dimer, which might be accounted for by the incorporation of additional protein subunits or RNA rather than PRC2 dimerization. Here we show that reconstituted human PRC2 is in fact a dimer, using multiple independent approaches including analytical size exclusion chromatography (SEC), SEC combined with multi-angle light scattering and co-immunoprecipitation of differentially tagged subunits. Even though it contains at least two RNA-binding subunits, each PRC2 dimer binds only one RNA molecule. Yet, multiple PRC2 dimers bind a single RNA molecule cooperatively. These observations suggest a model in which the first RNA binding event promotes the recruitment of multiple PRC2 complexes to chromatin, thereby nucleating repression.

Creator
Date Issued
  • 2014-08-01
Academic Affiliation
Journal Title
Journal Issue/Number
  • 14
Journal Volume
  • 42
File Extent
  • 9236-9248
Subject
Publisher
Last Modified
  • 2020-01-09
Identifier
  • PubMed ID: 24992961
Resource Type
Rights Statement
DOI
ISSN
  • 1362-4962
Language

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