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蛋白激酶CK2对酵母TBP的磷酸化作用降低了其与DNA的特异性结合。

Phosphorylation of yeast TBP by protein kinase CK2 reduces its specific binding to DNA.

作者信息

Maldonado E, Allende J E

机构信息

Programa de Biología Celular y Molecular, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Santiago.

出版信息

FEBS Lett. 1999 Jan 29;443(3):256-60. doi: 10.1016/s0014-5793(98)01734-7.

DOI:10.1016/s0014-5793(98)01734-7
PMID:10025943
Abstract

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.

摘要

蛋白激酶CK2是一种广泛存在的丝氨酸/苏氨酸激酶,它能使大量蛋白质磷酸化,包括几种转录因子。重组非洲爪蟾CK2能使重组酿酒酵母和粟酒裂殖酵母的TATA结合蛋白(TBP)磷酸化。CK2对TBP的磷酸化降低了其与TATA框的结合活性。CK2与来自HeLa细胞提取物的转录因子IID(TFIID)复合物共纯化,并使TFIID中的几种TBP相关因子磷酸化。这些发现共同表明,CK2通过调节TBP与TATA框的结合活性,在RNA聚合酶II控制转录过程中发挥作用。

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