A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1

David M. Keller, Xiaoya Zeng, Yun Wang, Qing Hong Zhang, Mini Kapoor, Hongjun Shu, Richard Goodman, Guillermina Lozano, Yingming Zhao, Hua Lu

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Abstract

Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not γ 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.

Original languageEnglish (US)
Pages (from-to)283-292
Number of pages10
JournalMolecular Cell
Volume7
Issue number2
DOIs
StatePublished - Jan 1 2001

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ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Keller, D. M., Zeng, X., Wang, Y., Zhang, Q. H., Kapoor, M., Shu, H., Goodman, R., Lozano, G., Zhao, Y., & Lu, H. (2001). A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Molecular Cell, 7(2), 283-292. https://doi.org/10.1016/S1097-2765(01)00176-9