Rb targets histone H3 methylation and HP1 to promoters

Soren J. Nielsen, Robert Schneider, Uta-Maria Bauer, Andrew J. Bannister, Ashby Morrison, Donal O'Carroll, Ron Firestein, Michael Cleary, Thomas Jenuwein, Rafael E. Herrera and Tony Kouzarides ()
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Soren J. Nielsen: Wellcome/CRC Institute and Department of Pathology
Robert Schneider: Wellcome/CRC Institute and Department of Pathology
Uta-Maria Bauer: Wellcome/CRC Institute and Department of Pathology
Andrew J. Bannister: Wellcome/CRC Institute and Department of Pathology
Ashby Morrison: Baylor College of Medicine, The Breast Center
Donal O'Carroll: Research Institute of Molecular Pathology (IMP), The Vienna Biocenter
Ron Firestein: Stanford University Medical Center
Michael Cleary: Stanford University Medical Center
Thomas Jenuwein: Research Institute of Molecular Pathology (IMP), The Vienna Biocenter
Rafael E. Herrera: Baylor College of Medicine, The Breast Center
Tony Kouzarides: Wellcome/CRC Institute and Department of Pathology

Nature, 2001, vol. 412, issue 6846, 561-565

Abstract: Abstract In eukaryotic cells the histone methylase SUV39H1 and the methyl-lysine binding protein HP1 functionally interact to repress transcription at heterochromatic sites1. Lysine 9 of histone H3 is methylated by SUV39H1 (ref. 2), creating a binding site for the chromo domain of HP1 (refs 3, 4). Here we show that SUV39H1 and HP1 are both involved in the repressive functions of the retinoblastoma (Rb) protein. Rb associates with SUV39H1 and HP1 in vivo by means of its pocket domain. SUV39H1 cooperates with Rb to repress the cyclin E promoter, and in fibroblasts that are disrupted for SUV39, the activity of the cyclin E and cyclin A2 genes are specifically elevated. Chromatin immunoprecipitations show that Rb is necessary to direct methylation of histone H3, and is necessary for binding of HP1 to the cyclin E promoter. These results indicate that the SUV39H1–HP1 complex is not only involved in heterochromatic silencing but also has a role in repression of euchromatic genes by Rb and perhaps other co-repressor proteins.

Date: 2001
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DOI: 10.1038/35087620

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