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Analysis of phosphorylation of wheat elongation factor 1 beta and beta' by casein kinase II
S Matsumoto1, T Mizoguchi, N Oizumi
1Institute for Cell Biology and Genetics, Faculty of Agriculture, Iwate University Morioka, Japan.
Bioscience, Biotechnology, and Biochemistry
|October 1, 1993
Abstract:
The purified casein kinase II (CK II) from Arabidopsis thaliana phosphorylates wheat elongation factor 1 beta (EF-1 beta), but not elongation factor 1 beta' (EF-1 beta'), which lacks a serine residue in the conserved phosphorylation site. Both EF-1 beta and beta' subunits, with similar functions, seem to undergo different regulation despite the partial amino acid sequence of EF-1 beta being similar to that of EF-1 beta'.