A phospholipid-stimulated protein kinase from Dictyostelium discoideum.
A protein kinase with unusual characteristics has been found in Dictyostelium discoideum. This kinase can use histone H1 as exogenous substrate, and the activity is stimulated by phospholipids, but not by Ca2+. This enzyme has been partially purified by using chromatography on DEAE-cellulose DE-52, spermine-agarose and phosphatidylserine-polyacrylamide. The protein kinase activity is very labile, even in the presence of protease inhibitors, making further purification difficult. In the activity-containing fractions, an endogenous protein of 140 kDa is labelled in vitro with [gamma-32P]ATP under conditions in which intramolecular rather than intermolecular reactions are favoured. This protein is labelled only in the presence of phospholipids, but not of Ca2+. We propose that the 140 kDa phosphoprotein might be the autophosphorylated enzyme.
Instituto de Investigaciones Biomedicas del C.S.I.C., Departamento de Bioquimica de la Facultad de Medicina de la U.A.M., Madrid, Spain.
B
B
Jiménez
A
A
Pestaña
M
M
Fernandez-Renart
D002847:Chromatography, Agarose; D002848:Chromatography, DEAE-Cellulose; D004023:Dictyostelium / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D010716:Phosphatidylinositols / Q000494:pharmacology; D010718:Phosphatidylserines / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*
D010716:Phosphatidylinositols; D010718:Phosphatidylserines; D010743:Phospholipids; D011494:Protein Kinases