Cloning, expression and properties of the alpha' subunit of casein kinase 2 from zebrafish (Danio rerio)

ANTONELLI M.; DANIOTTI J.L.; ROJO D.; ALLENDE C.C.; ALLENDE J.E.

Londres

Año: 1996 vol. 241 p. 272 - 272

he 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 (alpha and/or alpha´) and regulatory subunits (beta 2). The alpha and alpha´ subunits are encoded by different genes but are very similar in amino acid sequence, except that alpha´ is normally considerably shorter. There have been extensive biochemical studies with recombinant alpha and beta subunits of many species, but only one previous description of the activity of an isolated recombinant alpha´ subunit from human CK2 (Bodenbach, L., Fauss, J., Robitzki, A., Krehan, A., Lorenz, P., Lozeman, F. J. & Pyerin, W. (1994) Recombinant human casein kinase II. A study with the complete set of subunits (alpha, alpha´, and beta), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme, Eur. J. Biochem. 220, 263-273). In the present work, the isolation and bacterial exp