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 a subunit of class-q G-protein (42 kDa, CGqcz) which showed light-induced, dose-dependent binding to rhodopsin, and the other is an actin-like protein (44 kDa) with light-independent binding.

The primary structure of opsin of the crayfish ~roc~bar~ clarkii has been deduced from the cDNA sequence. The opsin is composed of 376 amino acid residues including all the conservative residues characteristic of other members of the rhodopsin family. Comparison of sequences of all known opsins reveals that the major Drosophila rhodopsin is more similar to the crayfish rhodopsin than to the Drosophila UV-sensitive pigments. The phylogenetic trees of invertebrate opsins are constructed.

Gq-type GTP-binding protein (Gq) plays an important role in invertebrate visual phototransduction. The subcellular localization of the alpha subunit of visual Gq in crayfish photoreceptor was investigated immunocytochemically and biochemically to demonstrate the details of the rhodopsin-Gq interaction. The localization of Gq(alpha) changed depending on the light condition. In the dark, Gq(alpha) was localized in the whole rhabdoms as the membrane-bound form. In the light, half of the Gq(alpha) was localized in the cytoplasm as the soluble form. The translocation of Gq(alpha) was reversible. The light-modulated translocation possibly controls the amount of Gq that can be activated by rhodopsin. In vitro hydroxylamine treatment of rhabdomeric membranes suggested that the translocation was regulated by the fatty-acid modification of Gq(alpha).

The semi-terrestrial sandhopper Talitrus saltator uses celestial visual cues to orient along the sea-land axis of the beach. Previous spectral-filtering experiments suggested that it perceives directional information from wavelengths in the ultraviolet (UV)-blue range. Binary choice experiments between dark and UV (380-nm) light carried out on dark-adapted individuals of T. saltator showed photopositive movement to UV. Morphologically, each ommatidium in the eye consists of five retinula cells, four large and one small. In electroretinogram experiments, sensitivity of the dark-adapted eye is dominated by a receptor maximally sensitive at about 390-450 nm and secondarily sensitive at about 500-550 nm. Selective light-adaptation experiments at 580 nm showed the apparent sensitivity decreasing at around the secondary sensitive range, thus disclosing the existence of UV-blue photoreceptor cells. Here the existence of UV-blue detection is confirmed, and evidence is provided that green and UV-blue visual pigments are located in the large and small retinula cells, respectively.

This paper deals with the structure and function of the intracerebral ocelli in the caudal area of the brain of the Japanese firefly. A pair of epilaterally placed specialized pigmented organs was found at the caudal ends of the brains of the fireflies Luciola cruciata and L. lateralis. On the basis of light and transmission electron micrographs of both male and female individuals these organs seemed photoreceptive in nature. Intracellular and extracellular recordings were obtained from the intracerebral ocelli of the fireflies with microelectrodes. The physiological evidence revealed that the cells found in the brain were, indeed, photoreceptors.