Abstract
Previously, we purified a UV-responsive p53 serine 392 kinase from F9 and HeLa cells and found that its activity is attributed to a high molecular weight protein complex containing the protein kinase CK2, along with the chromatin-associated factors hSPT16 and SSRP1. Here we determine that these proteins interact in vitro and in cells via non-overlapping domains and provide evidence consistent with the idea that hSPT16 and SSRP1 change the conformation of CK2 upon binding such that it specifically targets p53 over other substrates. Also, UV irradiation apparently induces the association of the complex, thereby increasing the specificity of CK2 for p53 at the expense of other cellular CK2 substrates and leading to an overall increase in p53 serine 392 phosphorylation.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Blotting, Western
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Casein Kinase II
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DNA / radiation effects*
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DNA Damage
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DNA-Binding Proteins / metabolism*
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Gene Deletion
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Glutathione Transferase / metabolism
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High Mobility Group Proteins / metabolism*
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Humans
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Kinetics
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Mice
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Models, Biological
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Models, Genetic
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Phosphorylation
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Plasmids / metabolism
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Protein Binding
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Protein Serine-Threonine Kinases / metabolism*
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / metabolism
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Serine / metabolism*
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Substrate Specificity
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Transcription Factors / metabolism*
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Transcriptional Elongation Factors*
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Transfection
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Tumor Cells, Cultured
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Tumor Suppressor Protein p53 / metabolism*
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Ultraviolet Rays
Substances
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DNA-Binding Proteins
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High Mobility Group Proteins
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Recombinant Fusion Proteins
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Recombinant Proteins
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SSRP1 protein, human
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Supt16 protein, mouse
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Transcription Factors
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Transcriptional Elongation Factors
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Tumor Suppressor Protein p53
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Ssrp1 protein, mouse
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Serine
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DNA
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Glutathione Transferase
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Casein Kinase II
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Protein Serine-Threonine Kinases