| First Author | Chuikov S | Year | 2004 |
| Journal | Nature | Volume | 432 |
| Issue | 7015 | Pages | 353-60 |
| PubMed ID | 15525938 | Mgi Jnum | J:345036 |
| Mgi Id | MGI:7581094 | Doi | 10.1038/nature03117 |
| Citation | Chuikov S, et al. (2004) Regulation of p53 activity through lysine methylation. Nature 432(7015):353-60 |
| abstractText | 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. |
