Abstract
Drosophila melanogaster casein kinase II (DmCKII) is composed of catalytic alpha and regulatory beta subunits associated as an alpha2beta2 heterotetramer. Using the two-hybrid system, we have screened a Drosophila embryo cDNA library for proteins that interact with DmCKII alpha. One of the cDNAs encodes a novel beta-like polypeptide, which we designate beta'. In situ hybridization localizes the corresponding gene to 56F1-2, a site distinct from that of both the beta gene and the Stellate family of beta-like sequences. The predicted sequence of beta' is more closely related to the beta subunit of Drosophila and other metazoans than to the Stellate family of proteins, suggesting that it is a second regulatory subunit. In vitro reconstitution studies show that a GST-beta' fusion protein associates with the alpha subunit to generate a tetrameric complex with regulatory properties similar to those of the native alpha2beta2 holoenzyme. The data are consistent with the proposed role of the beta' subunit as an integral component of the holoenzyme.
