期刊论文详细信息
FEBS Letters
Phosphorylation of yeast TBP by protein kinase CK2 reduces its specific binding to DNA
Allende, Jorge E1  Maldonado, Edio1 
[1] Programa de Biologı́a Celular y Molecular, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Casilla 70086, Santiago 7, Chile
关键词: Protein kinase CK2;    TBP phosphorylation;    TBP associated factor phosphorylation;    Binding activity;    CK2;    casein kinase II;    CK2α and CK2β;    the α and β subunits of protein kinase CK2;    TBP;    TATA binding protein;    TAF;    TBP associated factor;    TFIID;    transcription factor IID;    TFIIA;    transcription factor IIA;   
DOI  :  10.1016/S0014-5793(98)01734-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Protein kinase CK2 is a ubiquitous Ser/Thr kinase which phosphorylates a large number of proteins including several transcription factors. Recombinant Xenopus laevis CK2 phosphorylates both recombinant Saccharomyces cerevisiae and Schizosaccharomyces pombe TATA binding protein (TBP). The phosphorylation of TBP by CK2 reduces its binding activity to the TATA box. CK2 copurifies with the transcription factor IID (TFIID) complex from HeLa cell extracts and phosphorylates several of the TBP-associated factors within TFIID. Taken together these findings argue for a role of CK2 in the control of transcription by RNA polymerase II through the modulation of the binding activity of TBP to the TATA box.

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