Casein kinase II. cDNA sequences, developmental expression, and tissue distribution of mRNAs for alpha, alpha', and beta subunits of the chicken enzyme.

We report the complete primary structures, as deduced from cloned cDNAs, of two catalytic (alpha and alpha') and one beta subunit of chicken casein kinase II. The alpha and alpha' subunits are closely related to each other but differ in their carboxyl termini; moreover, minor differences are distributed throughout the entire lengths of the two proteins, indicating that they are derived from separate genes. Comparison of the chicken protein sequences with those of their mammalian homologs reveals a high degree of evolutionary conservation of all three subunits. Northern analyses were carried out to study the expression of casein kinase II subunits during chicken embryonic development as well as in adult tissues. A single transcript migrating at 1 kilobase was detected when using a beta-specific probe, but multiple transcripts ranging in size from 1.45 to 2.8 kilobase were revealed by alpha- and alpha'-specific probes. Expression of mRNA for all three subunits was high in early embryos but decreased substantially during embryonic development. A comparative analysis of casein kinase II expression in different adult tissues revealed two major findings. First, relative levels of expression of the two catalytic subunits displayed a pronounced tissue specificity, consistent with the possibility that alpha and alpha' subunits may carry out specialized functions. Second, no correlation was observed between levels of transcripts for the catalytic subunits and those of mRNA for the beta subunit.