作者: Homayoun Vaziri , Scott K. Dessain , Elinor Ng Eaton , Shin-Ichiro Imai , Roy A. Frye
DOI: 10.1016/S0092-8674(01)00527-X
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摘要: DNA damage-induced acetylation of p53 protein leads to its activation and either growth arrest or apoptosis. We show here that the product gene hSIR2(SIRT1), human homolog S. cerevisiae Sir2 known be involved in cell aging response damage, binds deacetylates with a specificity for C-terminal Lys382 residue, modification which has been implicated as transcription factor. Expression wild-type hSir2 cells reduces transcriptional activity p53. In contrast, expression catalytically inactive potentiates p53-dependent apoptosis radiosensitivity. propose is regulation function via deacetylation.