SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation

Alejandro Vaquero, Michael Scher, Hediye Erdjument-Bromage, Paul Tempst, Lourdes Serrano and Danny Reinberg ()
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Alejandro Vaquero: Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School
Michael Scher: Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School
Hediye Erdjument-Bromage: Molecular Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA
Paul Tempst: Molecular Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA
Lourdes Serrano: Human Genetics Institute, Rutgers University, 145 Bevier Road, Piscataway, New Jersey 08854, USA
Danny Reinberg: Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School

Nature, 2007, vol. 450, issue 7168, 440-444

Abstract: SUV39H1 is the major methyltransferase responsible for tri-methylation of histone H3 at lysine 9 in heterochromatin. The histone deacetylase SIRT1 is shown to target the SUV39H1 enzyme and contribute to elevated levels of SUV39H1 activity and H3K9me3 in heterochromatin.

Date: 2007
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DOI: 10.1038/nature06268

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