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Probing rhodopsin–transducin interaction using Drosophila Rh1–bovine rhodopsin chimeras
Journal article   Open access   Peer reviewed

Probing rhodopsin–transducin interaction using Drosophila Rh1–bovine rhodopsin chimeras

Michael Natochin, Brandy Barren, Syed Tariq Ahmad, Joseph E O’Tousa and Nikolai O Artemyev
Vision research (Oxford), Vol.46(27), pp.4575-4581
2006
DOI: 10.1016/j.visres.2006.07.013
PMID: 16979689
url
https://doi.org/10.1016/j.visres.2006.07.013View
Published (Version of record) Open Access

Abstract

Invertebrate and vertebrate rhodopsins share a low degree of homology and are coupled to G-proteins from different families. Here we explore the utility of fly-expressed chimeras between Drosophila rhodopsin Rh1 and bovine rhodopsin (Rho) to probe the interactions between the invertebrate and vertebrate visual pigments and their cognate G-proteins. Chimeric Rh1 pigments carrying individual substitutions of the cytoplasmic loops C2 and C3 and the C-terminus with the corresponding regions of Rho retained the ability to stimulate phototranduction in Drosophila, but failed to activate transducin. Surprisingly, chimeric Rho containing the Rh1 C-terminus was fully capable of transducin activation, indicating that the C-terminal domain of vertebrate rhodopsins is not essential for the functional coupling to transducin.
Transducin GPCR Rhodopsin Phototransduction Drosophila rhodopsin Rh1 G proteins

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