Abstract
In the first step of the visual transduction cascade, photoexcited rhodopsin (R*ret) binds to a GDP-carrying transducin (TGDP), allowing the release of the GDP from its site on T. We obtained a R*ret-Te complex (ret for retinal present, e for nucleotide site empty), undissociable almost indefinitely in a medium with physiological ionic strength. In this complex, rhodopsin is totally locked in the Meta-II conformation (R*ret). Incubation in a low ionic strength medium partially dissociates Te (probably a denatured form of transducin). In the presence of GDP, a R*ret-TGDP complex is obtained. TGDP appears to have a high binding affinity to R*ret in physiological ionic conditions. We show that the binding of Te or TGDP on cytoplasmic loops of rhodopsin induces different retroactions on the retinal site in rhodopsin.
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© 1992 Springer-Verlag Berlin Heidelberg
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Bornancin, F., Pfister, C. (1992). The Transitory Complexes Between Photoexcited Rhodopsin and Transducin. Biochemical and Spectroscopic Studies. In: Hargrave, P.A., Hofmann, K.P., Kaupp, U.B. (eds) Signal Transduction in Photoreceptor Cells. Research Reports in Physics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76482-0_8
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DOI: https://doi.org/10.1007/978-3-642-76482-0_8
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