Analysis of Phosphorylation of Wheat Elongation Factor 1β and β′ by Casein Kinase II

• Published in: Bioscience, biotechnology, and biochemistry Vol. 57; no. 10; pp. 1740 - 1742
• Main Authors: Matsumoto, Shogo, Mizoguchi, Tsuyoshi, Oizumi, Naoto, Tsuruga, Mie, Shinozaki, Kazuo, Taira, Hideharu, Ejiri, Shin-ichiro
• Format: Journal Article
• Language: English
• Published: Tokyo Taylor & Francis 1993; Japan Society for Bioscience Biotechnology and Agrochemistry
• Subjects: Amino Acid Sequence; Arabidopsis - enzymology; Biological and medical sciences; Biotechnology; Casein Kinases; Cloning, Molecular; DNA, Complementary - chemistry; Fundamental and applied biological sciences. Psychology; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Peptide Elongation Factor 1; Peptide Elongation Factors - chemistry; Peptide Elongation Factors - metabolism; Phosphorylation - drug effects; Protein Kinases - metabolism; Serine - chemistry; Translation. Translation factors. Protein processing; Triticum - chemistry; Phosphorylation; Enzyme; Protein kinase; Transferases; Wheat; In vitro; Aminoacid sequence; Structural analysis; Elongation factor EF1β
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.57.1740

The purified casein kinase II (CK II) from Arabidopsis thaliana phosphorylates wheat elongation factor Iβ (EF- Iβ), but not elongation factor Iβ' (EF-lβ'), which lacks a serine residue in the conserved phosphorylation site. Both EF-1β and1β' subunits, with similar functions, seem to undergo different regulation despite the partial amino acid sequence of EF-lβ being similar to that of EF-1β'.