The unique photochromic retinal protein from rhabdomeric octopus membranes – octopus rhodopsin (OctR) has emerged as promising material for biomolecular photonic applications due to its unique properties and advantages. Here we report isolation of the novel full length octR gene from retina cDNA of Octopus vulgaris eyes and its sequence comparison with rhodopsins of other cephalopods and vertebrates. The isolated gene can be used to develop various expression systems for production of recombinant OctR for structural studies and novel optobioelectronic applications. The alignment of amino acid (a.a.) sequence with different opsins revealed similarity to cephalopoda rhodopsins (Rho) and to human melanopsin from intrinsically photosensitive retinal ganglion cells. The alingment of OctR a.a. sequence with mammalian and cephalopoda Rho with known 3D structures revealed promising substitutions V2C and W292C for developing stable and functionally active recombinant OctR after heterologous expression.
A Novel Rhodopsin Gene from Octopus vulgaris for Optobioelectronics Materials
Pechkova, Eugenia;Nicolini, Claudio
2015-01-01
Abstract
The unique photochromic retinal protein from rhabdomeric octopus membranes – octopus rhodopsin (OctR) has emerged as promising material for biomolecular photonic applications due to its unique properties and advantages. Here we report isolation of the novel full length octR gene from retina cDNA of Octopus vulgaris eyes and its sequence comparison with rhodopsins of other cephalopods and vertebrates. The isolated gene can be used to develop various expression systems for production of recombinant OctR for structural studies and novel optobioelectronic applications. The alignment of amino acid (a.a.) sequence with different opsins revealed similarity to cephalopoda rhodopsins (Rho) and to human melanopsin from intrinsically photosensitive retinal ganglion cells. The alingment of OctR a.a. sequence with mammalian and cephalopoda Rho with known 3D structures revealed promising substitutions V2C and W292C for developing stable and functionally active recombinant OctR after heterologous expression.File | Dimensione | Formato | |
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