Article
A dimeric state for PRC2. Public Deposited
- 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
- 2020-11-09
- Identifier
- PubMed ID: 24992961
- Resource Type
- Rights Statement
- DOI
- ISSN
- 1362-4962
- Language
Relationships
- In Collection:
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Thumbnail | Title | Date Uploaded | Visibility | Actions |
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aDimericStateForPrc2.pdf | 2019-12-09 | Public | Download | |
nar03695R2013File009.pdf | 2019-12-09 | Public | Download |