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Phosphorylation of yeast TBP by protein kinase CK2 reduces its specific binding to DNA
Author(s) -
Maldonado Edio,
Allende Jorge E
Publication year - 1999
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/s0014-5793(98)01734-7
Subject(s) - transcription factor ii d , tata binding protein , transcription factor ii a , tata box binding protein , taf2 , transcription factor ii b , microbiology and biotechnology , chemistry , biology , biochemistry , transcription factor , dna binding protein , polymerase , promoter , dna , gene expression , gene , rna dependent rna polymerase , enhancer
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.