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. 2004 Nov 18;432(7015):353-60.
doi: 10.1038/nature03117. Epub 2004 Nov 3.

Regulation of p53 activity through lysine methylation

Sergei Chuikov  1 , 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, Danny Reinberg
Affiliations

Regulation of p53 activity through lysine methylation

Sergei Chuikov et al. Nature. .

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.

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