Polyamine binding activity of casein kinase II

Autor: Filhol, Odile, Cochet, Claude, Delagoutte, Thierry, Chambaz, Edmond M.
Zdroj: Biochemical and Biophysical Research Communications; October 1991, Vol. 180 Issue: 2 p945-952, 8p
Abstrakt: Protein phosphorylation by the ubiquitous casein kinase II (CKII) is known to be sensitive to naturally occuring polyamines. Using isolated recombinant α and β subunits of the kinase, as well as the α2β2oligomeric enzyme, it is shown that (i) CKII binds [3H]-spermine with Kds in the micromolar range. (ii) The β subunit appears mostly responsible for this binding activity. (iii) The isolated α (catalytic) subunit is not activated by polyamines. (iv) The polyamine-dependent activation of the oligomeric CKII requires the β subunit, which appears as a regulatory component in the native kinase. These observations suggest that there may be a functional interaction between polyamines and CKII in living cells, especially in the response to cell growth factors and trophic hormones.
Databáze: Supplemental Index