Journal
MOLECULAR CELL
Volume 7, Issue 2, Pages 283-292Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00176-9
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Funding
- NCI NIH HHS [R01 CA115468, R01 CA115468-05] Funding Source: Medline
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Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not gamma irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro. This kinase complex contains casein kinase 2 (CK2) and the chromatin transcriptional elongation factor FACT (a heterodimer of hSpt16 and SSRP1). In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53 over other substrates including casein. In addition, phosphorylation by the kinase complex enhances p53 activity. These results thus provide a potential mechanism for p53 activation by UV irradiation.
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