Analysis of phosphorylation of wheat elongation factor 1 beta and beta' by casein kinase II.
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'.
Matsumoto
S
S
Institute for Cell Biology and Genetics, Faculty of Agriculture, Iwate University Morioka, Japan.
Mizoguchi
T
T
Oizumi
N
N
Tsuruga
M
M
Shinozaki
K
K
Taira
H
H
Ejiri
S
S
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology; D047388:Casein Kinases; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry; D008969:Molecular Sequence Data; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D011494:Protein Kinases / Q000378:metabolism*; D012694:Serine / Q000737:chemistry; D014908:Triticum / Q000737:chemistry*
D018076:DNA, Complementary; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D012694:Serine; D011494:Protein Kinases; D047388:Casein Kinases