Enhancement of opsin activity by all-trans-retinal.

The rod cell photoreceptor apoprotein, opsin, activates the G-protein, transducin, although at a much reduced level than light-activated rhodopsin. The ability of all-trans-retinal to enhance opsin apoprotein activity was investigated using a guanyl nucleotide exchange assay on transducin. All-trans-retinal enhanced opsin activity in a concentration-dependent manner. At high concentrations of all-trans-retinal, the activity of the all-trans-retinal-opsin complex was comparable to that from an equimolar amount of metarhodopsin(II). However, in contrast to metarhodopsin(II), the active all-trans-retinalopsin complex did not require a stable Schiff base linkage between opsin and all-trans-retinal. The lack of a stable Schiff base and differences in activity at high pH imply that opsin and all-trans-retinal form a complex that is distinct from metarhodopsin(II). The ability of all-trans-retinal to stimulate the transduction cascade may be a source of post-bleach noise in photoreceptors.