Cloning, expression and properties of the α' subunit of case in kinase 2 from zebrafish (Danio rerio)

Abstract

The protein kinase casein kinase 2 (CK2) is ubiquitous in eukaryotic cells and is apparently involved in the control of cell division. The holoenzyme is a tetramer composed of two catalytic subunits (α and/or α') and regulatory subunits β2). The α and α' subunits are encoded by different genes but are very similar in amino acid sequence, except that α' is normally considerably shorter. There have been extensive biochemical studies with recombinant α and β subunits of many species, but only one previous description of the activity of an isolated recombinant α' subunit from human CK2 (Bodenbach, L., Fauss, J., Robitzki, A., Krehan, A., Lorenz, P., Lozeman, F.J. and Pyerin, W. (1994) Recombinant human casein kinase II. A study with the complete set of subunits (α, α', and β), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme, Eur. J. Biochem. 220, 263 -273). In the present work, the isolation and bacterial expression of a cDNA coding for the α' subunit o