Interaction of GTP‐binding protein Gq with photoactivated rhodopsin in the photoreceptor membranes of crayfish

FEBS Letters

Tashiro, Hideo¹  Terakita, Akihisa³  Katsukura, Yuki¹  Tsukahara, Yasuo²  Hariyama, Takahiko² 

[1] Photodynamics Research Center, The Institute of Chemical and Physical Research (RIKEN), Aoba-ku Koeji, Sendai 980, Japan;Graduate School of Information Sciences, Tohoku University, SKK Building, Sendai 980, Japan;Institute of Biology, Faculty of Education, Oita University, Oita 870-11, Japan

关键词: Photoreceptor membrane;    Rhodopsin;    G-protein;    Gq;    Signal transduction;    Phospholipase C;    Crayfish;    Procambarus clarkii;    ATPγS;    Adenosine 5'-O-[3-thiotriphosphate];    G-protein;    GTP-Binding protein;    GDPβS;    guanosine 5'O-[2-thiodiphosphate];    GTPγS;    guanosine 5'-O-[3-thiotriphosphate];    Gt;    rod transducin;    HPLC;    high-performance liquid chromatography;    PDE;    phosphodiesterase;    PLC;    phospholipase C;    SDS-PAGE;    sodium dodecyl sulphate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(93)80272-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interaction of G-protein with photoactivated rhodopsin (Rh^∗) in crayfish photoreceptor membranes was investigated by immunoprecipitation using an antibody against rhodopsin. Two kinds of protein were co-precipitated with rhodopsin. One is an α subunit of class-q G-protein (42 kDa, CGqα) which showed light-induced, dose-dependent binding to rhodopsin, and the other is an actin-like protein (44 kDa) with light-independent binding. Most of the CGqα was available for binding to Rh^∗ but was dissociated from Rh^∗ in the presence of GTPγS. These findings demonstrate that, in the crayfish photoreceptor, a Gq class of G-protein is activated by Rh^∗.

【 授权许可】

Unknown