Abstract
The long-wavelength-sensitive (LWS) opsins form one of four classes of vertebrate cone visual pigment and exhibit peak spectral sensitivities (λmax) that generally range from 525 to 560 nm for rhodopsin/vitamin-A1 photopigments. Unique amongst the opsin classes, many LWS pigments show anion sensitivity through the interaction of chloride ions with a histidine residue at site 197 (H197) to give a long-wavelength spectral shift in peak sensitivity. Although it has been shown that amino acid substitutions at five sites (180, 197, 277, 285 and 308) are useful in predicting the λmax values of the LWS pigment class, some species, such as the elephant shark and most marine mammals, express LWS opsins that possess λmax values that are not consistent with this ‘five-site’ rule, indicating that other interactions may be involved. This study has taken advantage of the natural mutation at the chloride-binding site in the mouse LWS pigment. Through the use of a number of mutant pigments generated by site-directed mutagenesis, a new model has been formulated that takes into account the role of charge and steric properties of the side chains of residues at sites 197 and 308 in the function of the chloride-binding site in determining the peak sensitivity of LWS photopigments.
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Acknowledgments
This work was supported by a grant from the BBSRC. We are grateful to Dr. Rosalie Crouch of the Storm Eye Institute, Medical University of South Carolina, USA, for the kind gift of 11-cis-retinal.
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Wayne I. L. Davies and Susan E. Wilkie contributed equally to this research.
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Davies, W.I.L., Wilkie, S.E., Cowing, J.A. et al. Anion sensitivity and spectral tuning of middle- and long-wavelength-sensitive (MWS/LWS) visual pigments. Cell. Mol. Life Sci. 69, 2455–2464 (2012). https://doi.org/10.1007/s00018-012-0934-4
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DOI: https://doi.org/10.1007/s00018-012-0934-4