Abstract

The mouse protein kinase CK2β subunit gene (Csnk2b) is composed of seven exons contained within 7874 bp. The exon and intron lengths extend from 76 to 321 and 111 to 1272 bp, respectively. The lengths of the murine coding exons correspond exactly to the lengths of the exons in the human CK2β gene. Both genes contain a first untranslated exon. Also, the promoter regions from the human and murine CK2β gene share some common features, e.g., they contain neither a TATA nor a CAAT box, exon 1 is flanked by a cluster of CpG dinucleotides and recognition sequences for the HpaII restriction endonuclease, and several blocks of sequence in the 5′ flanking region are conserved between mouse and human. Despite all of these common features, one of the most striking differences found concerns the human CK2α subunit binding domain at position -170 to -239 of the human gene. This domain has no counterpart in the murine gene. Hence, regulation of transcription of the CK2β gene by the catalytic CK2α subunit as was described by Robitzki et al. ( J. Biol. Chem. 268: 5694-5703, 1993) for the human gene cannot be considered a general regulatory mechanism.

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