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Regulation of p53 activity through lysine methylation.

Nature | Nov 18, 2004

http://www.ncbi.nlm.nih.gov/pubmed/15525938

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.

Pubmed ID: 15525938 RIS Download

Mesh terms: Amino Acid Sequence | Apoptosis | Cell Line | Cell Nucleus | Gene Expression Regulation | Genes, p53 | Genes, ras | Histone-Lysine N-Methyltransferase | Humans | Lysine | Methylation | Models, Molecular | Molecular Sequence Data | Promoter Regions, Genetic | Protein Binding | Protein Conformation | Protein Methyltransferases | RNA, Messenger | S-Adenosylhomocysteine | Substrate Specificity | Thermodynamics | Tumor Suppressor Protein p53

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