Regulation of p53 activity through lysine methylation

Sergei Chuikov, Julia K. Kurash, Jonathan R. Wilson, Bing Xiao, Neil Justin, Gleb S. Ivanov, Kristine McKinney, Paul Tempst, Carol Prives, Steven J. Gamblin, Nickolai A. Barlev () and Danny Reinberg ()
Additional contact information
Sergei Chuikov: Robert Wood Johnson Medical School
Julia K. Kurash: Molecular Oncology Research Institute, NEMC-Tufts School of Medicine
Jonathan R. Wilson: MRC-NIMR
Bing Xiao: MRC-NIMR
Neil Justin: MRC-NIMR
Gleb S. Ivanov: Molecular Oncology Research Institute, NEMC-Tufts School of Medicine
Kristine McKinney: Columbia University
Paul Tempst: Memorial Sloan Kettering Cancer Center
Carol Prives: Columbia University
Steven J. Gamblin: MRC-NIMR
Nickolai A. Barlev: Molecular Oncology Research Institute, NEMC-Tufts School of Medicine
Danny Reinberg: Robert Wood Johnson Medical School

Nature, 2004, vol. 432, issue 7015, 353-360

Abstract: Abstract p53 is a tumour suppressor that regulates the cellular response to genotoxic stresses. p53 is a short-lived protein and its activity is regulated mostly by stabilization via different post-translational modifications. Here we report a novel mechanism of p53 regulation through lysine methylation by Set9 methyltransferase. Set9 specifically methylates p53 at one residue within the carboxyl-terminus regulatory region. Methylated p53 is restricted to the nucleus and the modification positively affects its stability. Set9 regulates the expression of p53 target genes in a manner dependent on the p53-methylation site. The crystal structure of a ternary complex of Set9 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of p53 by this lysine methyltransferase.

Date: 2004
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DOI: 10.1038/nature03117

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