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A comparative study of rhodopsin function in the great bowerbird (Ptilonorhynchus nuchalis): spectral tuning and light-activated kinetics

van Hazel, Ilke, Dungan, Sarah Z., Hauser, Frances E., Morrow, James M., Endler, John A. and Chang, Belinda S.W. 2016, A comparative study of rhodopsin function in the great bowerbird (Ptilonorhynchus nuchalis): spectral tuning and light-activated kinetics, Protein science, vol. 25, no. 7, pp. 1308-1318, doi: 10.1002/pro.2902.

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Title A comparative study of rhodopsin function in the great bowerbird (Ptilonorhynchus nuchalis): spectral tuning and light-activated kinetics
Formatted title A comparative study of rhodopsin function in the great bowerbird (Ptilonorhynchus nuchalis): spectral tuning and light-activated kinetics
Author(s) van Hazel, Ilke
Dungan, Sarah Z.
Hauser, Frances E.
Morrow, James M.
Endler, John A.ORCID iD for Endler, John A. orcid.org/0000-0002-7557-7627
Chang, Belinda S.W.
Journal name Protein science
Volume number 25
Issue number 7
Start page 1308
End page 1318
Total pages 11
Publisher Wiley
Place of publication Hoboken, N.J.
Publication date 2016-07
ISSN 0961-8368
1469-896X
Keyword(s) passerine birds
evolution of vision
visual pigment
evolution of protein structure and function
comparative biochemistry
Summary Rhodopsin is the visual pigment responsible for initiating the phototransduction cascade in vertebrate rod photoreceptors. Although well-characterized in a few model systems, comparative studies of rhodopsin function, particularly for non-mammalian vertebrates are comparatively lacking. Bowerbirds are rare among passerines in possessing a key substitution, D83N, at a site that is otherwise highly conserved among G protein-coupled receptors. While this substitution is present in some dim-light adapted vertebrates, often accompanying another unusual substitution, A292S, its functional relevance in birds is uncertain. To investigate functional effects associated with these two substitutions, we use the rhodopsin gene from the great bowerbird (Ptilonorhynchus nuchalis) as a background for site-directed mutagenesis, in vitro expression and functional characterization. We also mutated these sites in two additional rhodopsins that do not naturally possess N83, chicken and bovine, for comparison. Both sites were found to contribute to spectral blue-shifts, but had opposing effects on kinetic rates. Substitutions at site 83 were found to primarily affect the kinetics of light-activated rhodopsin, while substitutions at site 292 had a larger impact on spectral tuning. The contribution of substitutions at site 83 to spectral tuning in particular depended on genetic background, but overall, the effects of substitutions were otherwise surprisingly additive, and the magnitudes of functional shifts were roughly similar across all three genetic backgrounds. By employing a comparative approach with multiple species, our study provides new insight into the joint impact of sites 83 and 292 on rhodopsin structure-function as well as their evolutionary significance for dim-light vision across vertebrates.
Language eng
DOI 10.1002/pro.2902
Field of Research 060899 Zoology not elsewhere classified
060399 Evolutionary Biology not elsewhere classified
0601 Biochemistry And Cell Biology
0802 Computation Theory And Mathematics
0899 Other Information And Computing Sciences
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2016, The Protein Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30083290

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