Light-induced binding of proteins to rhabdomeric membranes in the retina of crayfish (Procambarus clarkii).
Light-induced protein interaction as part of the process of visual transduction in arthropods with rhabdomeric photoreceptors was investigated biochemically by using crayfish retina. Two kinds of retinal buffer soluble proteins (one of 40 kDa and the other of 46 kDa) were found to bind to the irradiated rhabdomeric membranes both in vitro and in vivo. The proteins bound to the membranes in the presence of metarhodopsin. An antibody against mouse arrestin (S-antigen) cross-reacted with the 40 kDa protein. These results suggest that the binding of the proteins to the membranes is caused by the formation of metarhodopsin, and that the 40 kDa protein has a similar structure to arrestin.
Terakita
A
A
Laboratory for Photobiology, Institute of Chemical and Physical Research (RIKEN), Sendai, Japan.
Tsukahara
Y
Y
Hariyama
T
T
Seki
T
T
Tashiro
H
H
D000818:Animals; D000941:Antigens / Q000378:metabolism; D019393:Arrestin; D003400:Astacoidea / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D005136:Eye Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D008027:Light; D008970:Molecular Weight; D011485:Protein Binding / Q000528:radiation effects; D012160:Retina / Q000378:metabolism*; D012243:Rhodopsin / Q000031:analogs & derivatives / Q000378:metabolism; D017299:Rod Opsins / Q000378:metabolism
D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D017299:Rod Opsins; C013110:metarhodopsins; D012243:Rhodopsin