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Rhodopsin is a visual pigment ubiquitous in multicellular animals. If visual pigments have a common ancient origin, as is believed, then some unicellular organisms might also use a rhodopsin photoreceptor. We show here that the unicellular alga Chlamydomonas does indeed use a rhodopsin photoreceptor. We incorporated analogues of its retinal chromophore into(More)
The unicellular eukaryote Chlamydomonas reinhardtii is a phototactic alga that swims toward or away from light, using rhodopsin as the photopigment. The activity of retinal analogues was tested in the mutant FN68, which has high phototactic sensitivity only after incubation with retinal or analogues of retinal. Analogues prevented from isomerizing about the(More)
Retinal normally binds opsin forming the chromophore of the visual pigment, rhodopsin. In this investigation synthetic analogs were bound by the opsin of living cells of the alga Chlamydomonas reinhardtii; the effect was assayed by phototaxis to give an activation spectrum for each rhodopsin analog. The results show the influence of different chromophores(More)
A sensitive assay for the induction of carotenoid and rhodopsin synthesis, based on the phototactic response, has been developed in a mutant of the unicellular alga Chlamydomonas reinhardtii. In the dark, the mutant fails to synthesize carotene and retinal, but it contains the apoprotein opsin. When retinal synthesis is induced by light treatment, the(More)
RIIa is known as the dimerization and docking (D/D) domain of the cyclic AMP (cAMP)-dependent protein kinase. However, numerous molecules, including radial spoke protein 2 (RSP2) in Chlamydomonas flagella, also contain an RIIa or a similar DPY-30 domain. To elucidate new roles of D/D domain-containing proteins, we investigated a panel of RSP2 mutants. An(More)
The interaction of the bovine opsin apoprotein with transducin in rod outer segment membranes was investigated using a guanyl nucleotide exchange assay. In exhaustive binding experiments, opsin activates transducin, with half-maximal exchange activity occurring at 0.8 mol of opsin/mol of transducin. The opsin activity was light-insensitive,(More)
Chlamydomonas reinhardtii swims toward or away from light (phototaxis) in a graded way depending on various conditions. Activation of rhodopsin provides signals to control the steering of this unicellular organism relative to a light source and to up-regulate rhodopsin biosynthesis. Intracellular cAMP and cGMP concentrations were measured in positive (1117,(More)
Rhodopsin is the general name for a family of visual pigments that receive light and transmit this signal to the rest of an organism. Chlamydomonas reinhardtii is a unicellular eukaryote whose light-tracking system consists of a single eye. Through spectral studies of Chlamydomonas' reaction to light of different wavelengths (action spectroscopy), it has(More)