[Phosphorylation of tryptophanyl-tRNA-synthase in extracts of bovine pancreas].
The polypeptide with a mobility of the tryptophanyl-tRNA-synthetase subunit can be labeled in bovine pancreas extracts from [gamma-32P]ATP. Immunoprecipitation analysis with monospecific polyclonal antibodies against the enzyme as well as identification of [32P]phosphoamino acids in the immunoprecipitate revealed that in bovine pancreas extracts tryptophanyl-tRNA-synthetase undergoes phosphorylation at serine residues. The level of phosphorylation does not change in the presence of activity modulators of cAMP-, cGMP- and Ca2(+)-dependent protein kinases, decreases after addition of phosphoseryl/phosphothreonyl-protein phosphatase inhibitors and increases in the presence of their activators. It was supposed that phosphorylation of tryptophanyl-tRNA-synthetase catalyzed by seryl/threonyl-specific protein kinase depends on the activity of phosphoseryl/phosphothreonyl-phosphatase.
Zargarova
T A
TA
Aleksandrova
N M
NM
Paleĭ
E L
EL
Favorova
O O
OO
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002417:Cattle; D010179:Pancreas / Q000201:enzymology*; D010184:Pancreatic Extracts / Q000737:chemistry*; D010191:Pancreatic Polypeptide / Q000096:biosynthesis; D010766:Phosphorylation; D011233:Precipitin Tests; D012694:Serine / Q000737:chemistry; D014369:Tryptophan-tRNA Ligase / Q000378:metabolism*
D010184:Pancreatic Extracts; D012694:Serine; D010191:Pancreatic Polypeptide; D000255:Adenosine Triphosphate; D014369:Tryptophan-tRNA Ligase
Fosforilirovanie triptofanil-tRNK-sintetazy v ékstraktakh podzheludochnoĭ zhelezy krupnogo rogatogo skota.