The effect of phosphorylation of the EF-2 isolated from rat liver cells on protein biosynthesis in vitro.
The activity of EF-2 was distinctly decreased after phosphorylation catalysed by a partly purified calmodulin and Ca2+ dependent protein kinase III. At the same time 32P from [gamma-32P]ATP was incorporated into EF-2 molecule. After dephosphorylation of EF-2 catalysed by alkaline phosphatase the activity of this factor was increased. This suggests that the phosphorylation-dephosphorylation of EF-2 is the regulatory process in the elongation step of the translation. Preliminary purification of the kinase III from rat liver resulted in 8-fold purified enzyme with a recovery of 60%.
Gajko
A
A
Department of General and Organic Chemistry, Institute of Chemistry, Medical Academy, Białystok, Poland.
Sredzińska
K
K
Marcinkiewicz
C
C
Gałasiński
W
W
D000818:Animals; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000096:biosynthesis / Q000378:metabolism*; D010750:Phosphoproteins / Q000096:biosynthesis / Q000378:metabolism*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000302:isolation & purification; D051381:Rats; D012269:Ribosomal Proteins / Q000096:biosynthesis / Q000378:metabolism*
D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010750:Phosphoproteins; D012269:Ribosomal Proteins; D010770:Phosphotransferases