Study of phosphorylation of translation elongation factor 2 (EF-2) from wheat germ

• Published in: FEBS letters Vol. 321; no. 2; pp. 219 - 223
• Main Authors: Smailov, Salim K., Lee, Anatoly V., Iskakov, Bulat K.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 26-04-1993; Elsevier
• Subjects: Amino Acid Sequence; Animals; Autoradiography; Biological and medical sciences; Calcium-Calmodulin-Dependent Protein Kinases; Cell-Free System; Electrophoresis, Gel, Two-Dimensional; Elongation factor 2; Elongation Factor 2 Kinase; Fundamental and applied biological sciences. Psychology; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Molecular Weight; Peptide Biosynthesis; Peptide Elongation Factor 2; Peptide Elongation Factors - isolation & purification; Peptide Elongation Factors - metabolism; Peptides; Phosphoproteins - isolation & purification; Phosphoproteins - metabolism; Phosphoric Monoester Hydrolases - metabolism; Phosphorus Radioisotopes; Phosphorylation; Poly U - metabolism; Protein Biosynthesis; Protein Kinases - metabolism; Protein phosphorylation; Regulation of translation; Seeds - metabolism; Sequence Homology, Amino Acid; Translation. Translation factors. Protein processing; Trifluoperazine - pharmacology; Triticum - metabolism; Triticum aestivum; Wheat germ; Wheat germ; Regulation of translation; Protein phosphorylation; Triticum aestivum; Elongation factor 2; Monocotyledones; Phosphorylation; Regulation(control); Gramineae; Angiospermae; Elongation factor EF2; Spermatophyta; Genetical translation; In vitro
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(93)80112-8

Phosphorylation of elongation factor 2 (EF-2) by specific Ca
2+/calmodulin-dependent kinase is considered as a possible mechanism of regulation of protein biosynthesis in animal cells at the level of polypeptide chain elongation. In this report we show that wheat germ EF-2 can be intensively phosphorylated by the rabbit reticulocyte EF-2 kinase. Phosphorylation results in inhibition of the activity of plant EF-2 in poly(U)-dependent cell-free translation system. Thus, the activity of EF-2 in plant cells can be potentially regulated by phosphorylation. However, we could not detect endogenous EF-2 kinase activity in wheat germ either in vitro or in vivo. Furthermore, EF-2 kinase activity is not displayed in different organs of wheat and other higher plants.