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Identification of three protein kinases which phosphorylate threonyl‐tRNA synthetase from rat liver
Author(s) -
Pendergast Ann Marie,
Traugh Jolinda A.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81007-9
Subject(s) - kinase , phosphorylation , biochemistry , identification (biology) , chemistry , biology , microbiology and biotechnology , botany
Threonyl‐tRNA synthetase is phosphorylated in Chinese hamster ovary cells labeled with 2 P i [(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 Ca 2+ , 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.