A DNA Damage–Induced p53 Serine 392 Kinase Complex Contains CK2, hSpt16, and SSRP1

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...

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Bibliographic Details
Published inMolecular cell Vol. 7; no. 2; pp. 283 - 292
Main Authors Keller, David M, Zeng, Xiaoya, Wang, Yun, Zhang, Qing Hong, Kapoor, Mini, Shu, Hongjun, Goodman, Richard, Lozano, Guillermina, Zhao, Yingming, Lu, Hua
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.02.2001
Subjects
Amino Acid Sequence
casein kinase 2
Casein Kinase II
Cell Cycle Proteins - metabolism
Chromatography, Gel
Conserved Sequence
DNA Damage - genetics
DNA-Binding Proteins - metabolism
Enzyme Activation - radiation effects
FACT protein
High Mobility Group Proteins - metabolism
Humans
Macromolecular Substances
Molecular Sequence Data
Molecular Weight
p21-Activated Kinases
P53 protein
Phosphorylation
Phosphoserine - metabolism
Protein Binding
Protein-Serine-Threonine Kinases - chemistry
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - isolation & purification
Protein-Serine-Threonine Kinases - metabolism
Sequence Alignment
Substrate Specificity
Transcription Factors
Transcription, Genetic
Transcriptional Elongation Factors
Tumor Cells, Cultured
Tumor Suppressor Protein p53 - metabolism
Ultraviolet Rays
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Summary: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.
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ISSN:1097-2765
1097-4164
DOI:10.1016/S1097-2765(01)00176-9