Participation of GTP-binding protein in the photo-transduction of Paramecium bursaria.
Analysis of the flow of light information in Paramecium, especially the participation of GTP-binding protein, was carried out. Injection of GDP-beta-S into Paramecium cell abolished the light-induced inward current. The partially purified rhodopsin-like protein (RLP) that we obtained activated frog rod outer segments (ROS) GTPase. A GTP-binding protein, with Mw 57,000 was detected by immunostaining with anti-rat G alpha rabbit IgG. These results suggest that the light information flows from the light-captured RLP to the GTP-binding protein.
Shinozawa
T
T
Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University, Japan.
Hashimoto
H
H
Fujita
J
J
Nakaoka
Y
Y
D000818:Animals; D004789:Enzyme Activation; D020558:GTP Phosphohydrolases / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000031:analogs & derivatives / Q000494:pharmacology; D055537:Light Signal Transduction; D010247:Paramecium / Q000378:metabolism*; D015800:Protozoan Proteins / Q000378:metabolism*; D011817:Rabbits; D011898:Ranidae; D012243:Rhodopsin / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000201:enzymology; D013873:Thionucleotides / Q000494:pharmacology
D015800:Protozoan Proteins; D013873:Thionucleotides; D006153:Guanosine Diphosphate; C023427:guanosine 5'-O-(2-thiodiphosphate); D012243:Rhodopsin; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins