Regulation of the DNA binding of p53 by its interaction with protein kinase CK2

FEBS Lett. 1997 May 12;408(1):99-104. doi: 10.1016/s0014-5793(97)00399-2.

Abstract

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 beta-subunit of protein kinase CK2. Using a p53-specific DNA binding element we found that the beta-subunit of CK2 inhibited the DNA binding of p53 whereas the alpha-subunit had no influence. The CK2 holoenzyme consisting of two alpha- and two beta-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 beta-subunit of CK2 on the DNA binding activity of p53.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Casein Kinase II
  • Cell Line
  • DNA / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Humans
  • Phosphorylation
  • Protein Conformation
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / metabolism*
  • Recombinant Proteins / metabolism
  • Spodoptera
  • Tumor Suppressor Protein p53 / immunology
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • Antibodies, Monoclonal
  • Recombinant Proteins
  • Tumor Suppressor Protein p53
  • DNA
  • Casein Kinase II
  • Protein-Serine-Threonine Kinases