Work

Identification of three protein kinases which phosphorylate threonyl‐tRNA synthetase from rat liver

Year: 1986

Type: article

Abstract: Threonyl-tRNA synthetase is phosphorylated in Chinese hamster ovary cells labeled with 32Pi [(1984) J. Biol. Chem. 259, 11160-11161]. Phosphorylation of the purified synthetase from rat liver has been examined with five different protein kinases. Three of the enzymes phosphorylate the synthetase, protease activated kinase I, the cAMP-dependent protein kinase, and the Ca2+, phospholipid-dependent protein kinase. Phosphorylation occurs exclusively on seryl residues. Two-dimensional phosphopeptide maps of tryptic digests of the phosphorylated synthetase are distinct with each protein kinase. These data suggest that multiple phosphorylation of the synthetase may occur in vivo.

Source: FEBS Letters

DOI: 10.1016/0014-5793(86)81007-9

Authors: Ann Marie Pendergast, Jolinda A. Traugh

Institution: University of California, Riverside

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: University of Connecticut, National Institute of General Medical Sciences

Award: G2587967589