Polylysine activates membrane-bound adenylyl cyclase from Xenopus laevis oocytes through the Gs transducing protein.
1. The activity of the adenylyl cyclase found in the membranes of Xenopus laevis can be affected by polylysine and other polycations. 2. The activity of the catalytic subunit measured with forskolin is inhibited by polylysine and polyarginine at concentrations above 10 microM and by spermine above 3 mM. 3. The adenylyl cyclase activity stimulated by GTP-gamma-S or F- through the stimulatory G protein (Gs) can be increased by polylysine, polyornithine and spermine but not by polyarginine. 4. Polylysine stimulation of Gs dependent activity is due to the increase in the apparent affinity for GTP-gamma-S and to a lowering of the requirement for Mg2+ concentration.
Antonelli
M
M
Departamento de Bioquímica, Facultad de Medicina, Universidad de Chile, Santiago.
Olate
J
J
Allende
C C
CC
Allende
J E
JE
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004789:Enzyme Activation; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000378:metabolism*; D009865:Oocytes / Q000201:enzymology*; D010455:Peptides / Q000502:physiology; D011107:Polylysine / Q000502:physiology*; D015398:Signal Transduction; D014982:Xenopus laevis
D010455:Peptides; D011107:Polylysine; C015462:polyarginine; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D000262:Adenylyl Cyclases