Regulation of adenylyl cyclase from Blastocladiella emersonii by guanine nucleotides.
GTP gamma S stimulates adenylyl cyclase in particulate fractions of Blastocladiella emersonii zoospores. Cholera toxin catalyses the ADP-ribosylation of a membrane protein of a molecular weight (46,000) similar to that of the alpha subunit of Gs found in vertebrate cells. A membrane protein of 46 kDa can also be recognized in Western blots by an antipeptide antiserum (RM/1) raised against the C-terminus of G alpha 2-subunits. These results suggest that a G-protein mediates the regulation of Blastocladiella adenylyl cyclase by guanine nucleotides.
Terenzi
H
H
Departamento de Bioquímica, Universidade de São Paulo, Brazil.
Maia
J C
JC
D000244:Adenosine Diphosphate / Q000378:metabolism; D000067956:Adenylyl Cyclase Inhibitors; D000262:Adenylyl Cyclases / Q000378:metabolism*; D001754:Blastocladiella / Q000201:enzymology* / Q000502:physiology; D015153:Blotting, Western; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006150:Guanine Nucleotides / Q000378:metabolism*; D006358:Hot Temperature; D015151:Immunoblotting; D013172:Spores, Fungal
D000067956:Adenylyl Cyclase Inhibitors; D006150:Guanine Nucleotides; D000244:Adenosine Diphosphate; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases