Analysis of interactions between the subunits of protein kinase CK2.

Protein kinase CK2, which was formerly known as casein kinase II, is a highly conserved protein serine/threonine kinase implicated in the control of cell proliferation through its phosphorylation of regulatory nuclear proteins. The enzyme consists of catalytic (alpha and (or) alpha') subunits and beta subunits that modulate the activity of the catalytic subunits. These subunits are arranged in homotetrameric (i.e., alpha 2 beta 2 or alpha' 2 beta 2) or heterotetrameric (i.e., alpha alpha' beta 2) complexes. We previously demonstrated using the yeast two-hybrid system that alpha (or alpha') subunits can interact with beta subunits but not other alpha (or alpha') subunits. By comparison, beta subunits can interact with alpha (or alpha') and with beta subunits, suggesting that the protein kinase CK2 holoenzyme forms because of the ability of beta subunits to dimerize, bringing two heterodimers (alpha beta or alpha' beta) into a tetrameric complex. In the present study, we used the yeast two-hybrid system to examine the domains of interactions between the alpha and beta subunits of protein kinase CK2. These studies indicate that the ability of beta to interact with alpha resides within the carboxy-terminal domain of beta. By comparison, our studies suggest that individual domains of alpha are not sufficient for interactions with beta.