Role of the polycomb protein EED in the propagation of repressive histone marks

Raphael Margueron, Neil Justin, Katsuhito Ohno, Miriam L. Sharpe, Jinsook Son, William J. Drury, Philipp Voigt, Stephen R. Martin, William R. Taylor, Valeria De Marco, Vincenzo Pirrotta (), Danny Reinberg () and Steven J. Gamblin ()
Additional contact information
Raphael Margueron: New York University Medical School, 522 First Avenue, New York, New York 10016, USA
Neil Justin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Katsuhito Ohno: Rutgers University, Nelson Laboratories, 604 Allison Road, Piscataway, New Jersey 08854, USA
Miriam L. Sharpe: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Jinsook Son: New York University Medical School, 522 First Avenue, New York, New York 10016, USA
William J. Drury: New York University Medical School, 522 First Avenue, New York, New York 10016, USA
Philipp Voigt: New York University Medical School, 522 First Avenue, New York, New York 10016, USA
Stephen R. Martin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
William R. Taylor: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Valeria De Marco: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Vincenzo Pirrotta: Rutgers University, Nelson Laboratories, 604 Allison Road, Piscataway, New Jersey 08854, USA
Danny Reinberg: New York University Medical School, 522 First Avenue, New York, New York 10016, USA
Steven J. Gamblin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

Nature, 2009, vol. 461, issue 7265, 762-767

Abstract: Abstract Polycomb group proteins have an essential role in the epigenetic maintenance of repressive chromatin states. The gene-silencing activity of the Polycomb repressive complex 2 (PRC2) depends on its ability to trimethylate lysine 27 of histone H3 (H3K27) by the catalytic SET domain of the EZH2 subunit, and at least two other subunits of the complex: SUZ12 and EED. Here we show that the carboxy-terminal domain of EED specifically binds to histone tails carrying trimethyl-lysine residues associated with repressive chromatin marks, and that this leads to the allosteric activation of the methyltransferase activity of PRC2. Mutations in EED that prevent it from recognizing repressive trimethyl-lysine marks abolish the activation of PRC2 in vitro and, in Drosophila, reduce global methylation and disrupt development. These findings suggest a model for the propagation of the H3K27me3 mark that accounts for the maintenance of repressive chromatin domains and for the transmission of a histone modification from mother to daughter cells.

Date: 2009
References: Add references at CitEc
Citations: View citations in EconPapers (6)

Downloads: (external link)
https://www.nature.com/articles/nature08398 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:461:y:2009:i:7265:d:10.1038_nature08398

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature08398

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().