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Regulation of the DNA binding of p53 by its interaction with protein kinase CK2
Author(s) -
Prowald Alexandra,
Schuster Norbert,
Montenarh Mathias
Publication year - 1997
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(97)00399-2
Subject(s) - protein subunit , microbiology and biotechnology , specificity factor , interleukin 10 receptor, alpha subunit , gamma aminobutyric acid receptor subunit alpha 1 , casein kinase 2 , biochemistry , dna , chemistry , biology , protein kinase a , kinase , mitogen activated protein kinase kinase , g alpha subunit , gene , polymerase , rna dependent rna polymerase
Some of the numerous functions of the growth suppressor protein p53 are regulated by its interaction with viral and cellular proteins. C‐terminal sequences of p53 are implicated in binding to the regulatory β‐subunit of protein kinase CK2. Using a p53‐specific DNA binding element we found that the β‐subunit of CK2 inhibited the DNA binding of p53 whereas the α‐subunit had no influence. The CK2 holoenzyme consisting of two α‐ and two β‐subunits led to a supershift in DNA binding of p53 similar to the p53‐specific monoclonal antibody PAb421 as well as the C‐terminus of p53. Thus, our results showed an individual role of the free β‐subunit of CK2 on the DNA binding activity of p53.