Phosphorylation of the N‐terminal domain of Xenopus TATA‐box binding protein by DNA‐dependent protein kinase depends on the C‐terminal core domain

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Abstract
DNA‐dependent protein kinase (DNA‐PK) has been shown to phosphorylate several transcription factors in vitro, suggesting that this nuclear enzyme — in addition to its role in DNA repair and recombination — may be involved in transcriptional regulation. In the typical mechanism the DNA‐bound kinase phosphorylates a substrate that is bound to the same DNA molecule. Here I report that the Xenopus TATA‐box binding protein (xTBP) is hyperphosphorylated by DNA‐PK in vitro. The phosphorylation is in the N‐terminal domain of the protein but depends fully on the presence of the C‐terminal core domain.