Journal
CELL
Volume 107, Issue 2, Pages 149-159Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00527-X
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Funding
- NCI NIH HHS [R01 CA78461] Funding Source: Medline
- NHLBI NIH HHS [K08HL04463] Funding Source: Medline
- NINDS NIH HHS [NS34746] Funding Source: Medline
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DNA damage-induced acetylation of p53 protein leads to its activation and either growth arrest or apoptosis. We show here that the protein product of the gene hSIR2(SIRT1), the human homolog of the S. cerevisiae Sir2 protein known to be involved in cell aging and in the response to DNA damage, binds and deacetylates the p53 protein with a specificity for its C-terminal Lys382 residue, modification of which has been implicated in the activation of p53 as a transcription factor. Expression of wild-type hSir2 in human cells reduces the transcriptional activity of p53. In contrast, expression of a catalytically inactive hSir2 protein potentiates p53-dependent apoptosis and radiosensitivity. We propose that hSir2 is involved in the regulation of p53 function via deacetylation.
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