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Phosphorylation of the N‐terminal domain of Xenopus TATA‐box binding protein by DNA‐dependent protein kinase depends on the C‐terminal core domain
Author(s) -
Labhart Paul
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00420-6
Subject(s) - hmg box , tata binding protein , tata box , xenopus , microbiology and biotechnology , tata box binding protein , protein kinase a , biology , dna clamp , biochemistry , chemistry , phosphorylation , transcription factor , dna binding protein , gene , promoter , gene expression , rna , reverse transcriptase
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.