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

FEBS Letters

Labhart, Paul¹ 

[1] The Scripps Research Institute, Department for Molecular and Experimental Medicine, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA

关键词: DNA-dependent protein kinase;    TATA-box binding protein;    Xenopus laevis;   

DOI  :  10.1016/0014-5793(96)00420-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown