Protein kinase CK2 interacts with a multi-protein binding domain of p53.
p53 is one of the most powerful negative regulators of growth. To manage this in an efficient way it has to interact with a set of different cellular proteins. Most contacts with the cellular environment occur in the N- or the C-terminal domain of the protein. Since we previously found that p53 binds to the regulatory beta-subunit of CK2 we now analyzed N- and C-terminal domains of p53 separately for the binding of protein kinase CK2, an enzyme which seems to have a certain importance for proliferation processes. With different overlay assays we could map the binding domain of protein kinase CK2 to a sequence between amino acids 325-344, a region which coincides with the interaction domain of some other p53 binding proteins. We also found that the regulatory beta-subunit of protein kinase CK2 binds independent of the catalytic alpha-subunit to this C-terminal domain of p53.
Götz
C
C
Medical Biochemistry, University of the Saarland, Homburg, Germany.
Scholtes
P
P
Prowald
A
A
Schuster
N
N
Nastainczyk
W
W
Montenarh
M
M
D000595:Amino Acid Sequence; D001667:Binding, Competitive; D047390:Casein Kinase II; D020134:Catalytic Domain; D006801:Humans; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000378:metabolism*
D016159:Tumor Suppressor Protein p53; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases