• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


Regulation of p53 activity through lysine methylation.

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


  • Chuikov S
  • Kurash JK
  • Wilson JR
  • Xiao B
  • Justin N
  • Ivanov GS
  • McKinney K
  • Tempst P
  • Prives C
  • Gamblin SJ
  • Barlev NA
  • Reinberg D



Publication Data

November 18, 2004

Associated Grants


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