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Activation of the p53 tumour suppressor protein in response to DNA damage leads to apoptosis or cell-cycle arrest. Enzymatic modifications are widely believed to affect and regulate p53 activity. We describe here a level of post-translational control that has an important functional consequence on the p53 response. We show that the protein arginine methyltransferase (PRMT) 5, as a co-factor in a DNA damage responsive co-activator complex that interacts with p53, is responsible for methylating p53. Arginine methylation is regulated during the p53 response and affects the target gene specificity of p53. Furthermore, PRMT5 depletion triggers p53-dependent apoptosis. Thus, methylation on arginine residues is an underlying mechanism of control during the p53 response.

Original publication

DOI

10.1038/ncb1802

Type

Journal article

Journal

Nat Cell Biol

Publication Date

12/2008

Volume

10

Pages

1431 - 1439

Keywords

Amino Acid Sequence, Apoptosis, Arginine, Carrier Proteins, HeLa Cells, Humans, Methylation, Molecular Sequence Data, Mutant Proteins, Protein Binding, Protein Methyltransferases, Protein Structure, Quaternary, Protein Transport, Protein-Arginine N-Methyltransferases, Tumor Suppressor Protein p53