Phosphorylation of the N-terminal domain of Xenopus TATA-box binding protein by DNA-dependent protein kinase depends on the C-terminal core domain.
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.
Labhart
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Scripps Research Institute, Department for Molecular and Experimental Medicine, La Jolla, CA 92037, USA.plabhart@scripps.edu
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D051747:DNA-Activated Protein Kinase; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D013329:Structure-Activity Relationship; D016385:TATA Box; D035181:TATA-Box Binding Protein; D014157:Transcription Factors / Q000378:metabolism*; D014982:Xenopus laevis
D004268:DNA-Binding Proteins; D035181:TATA-Box Binding Protein; D014157:Transcription Factors; D004247:DNA; D051747:DNA-Activated Protein Kinase; D017346:Protein Serine-Threonine Kinases