Abstract
The purified casein kinase II (CK II) from Arabidopsis thaliana phosphorylates wheat elongation factor 1β (EF-1β), but not elongation factor 1β' (EF-1β'), which lacks a serine residue in the conserved phosphorylation site. Both EF-1β and β' subunits, with similar functions, seem to undergo different regulation despite the partial amino acid sequence of EF-1β being similar to that of EF-1β'.