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Functional expression and characterization of frog photoreceptor-specific calcium-binding proteins.

S-modulin (sensitivity-modulating protein) is a photoreceptor-specific calcium-binding protein which plays an important role in the light adaptation process by controlling rhodopsin phosphorylation in rods. S-modulin and its cone homologue, s26, were expressed at high level (more than 30% of total protein) in Escherichia coli and then purified. They both inhibited rhodopsin phosphorylation in a calcium dependent manner. Myristoylated recombinants of S-modulin and s26 showed calcium-dependent changes in tryptophan emission spectra with half-maxima at about 0.7 microM free calcium concentration. However, the spectral changes are distinctive from each other, suggesting that there is some difference in the structural change between S-modulin and s26.