The pyruvate dehydrogenase complex of Saccharomyces cerevisiae is regulated by phosphorylation.
Mitochondria were isolated from Saccharomyces cerevisiae grown on different carbon sources prior to incubation with [gamma-32P]ATP. A major 46,000-M(r) phosphoprotein, corresponding in M(r) value to the E1 alpha subunit of the yeast pyruvate dehydrogenase complex (PDC), was detected only in mitochondria isolated from cells grown on a fermentable carbon source such as galactose. Immunoprecipitation with subunit-specific antiserum to the E1 component of mammalian or yeast PDC confirmed the identity of this polypeptide. PDC activity in isolated yeast mitochondria could be inactivated in an ATP-dependent fashion and reactivated in the presence of Ca2+ ions.
James
A G
AG
Division of Biochemistry and Molecular Biology, University of Glasgow, Scotland, UK.
Cook
R M
RM
West
S M
SM
Lindsay
J G
JG
D000255:Adenosine Triphosphate / Q000378:metabolism; D001345:Autoradiography; D002118:Calcium / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006706:Homeostasis; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011768:Pyruvate Dehydrogenase Complex / Q000302:isolation & purification / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D010750:Phosphoproteins; D010761:Phosphorus Radioisotopes; D011768:Pyruvate Dehydrogenase Complex; D000255:Adenosine Triphosphate; D002118:Calcium