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 th is 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 th e C-terminal domain of the protein. Since we previously found that p53 bind s to the regulatory beta-subunit of CK2 we now analyzed N- and C-terminal d omains of p53 separately for the binding of protein kinase CK2, an enzyme w hich seems to have a certain importance for proliferation processes. With d ifferent overlay assays we could map the binding domain of protein kinase C K2 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 t hat the regulatory beta-subunit of protein kinase CK2 binds independent of the catalytic alpha-subunit to this C-terminal domain of p53.