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Molecular characterization of crustacean visual pigments and the evolution of pancrustacean opsins.
Mol Biol Evol. 2007 Jan; 24(1):253-68.MB

Abstract

Investigations of opsin evolution outside of vertebrate systems have long been focused on insect visual pigments, whereas other groups have received little attention. Furthermore, few studies have explicitly investigated the selective influences across all the currently characterized arthropod opsins. In this study, we contribute to the knowledge of crustacean opsins by sequencing 1 opsin gene each from 6 previously uncharacterized crustacean species (Euphausia superba, Homarus gammarus, Archaeomysis grebnitzkii, Holmesimysis costata, Mysis diluviana, and Neomysis americana). Visual pigment spectral absorbances were measured using microspectrophotometry for species not previously characterized (A. grebnitzkii=496 nm, H. costata=512 nm, M. diluviana=501 nm, and N. americana=520 nm). These novel crustacean opsin sequences were included in a phylogenetic analysis with previously characterized arthropod opsin sequences to determine the evolutionary placement relative to the well-established insect spectral clades (long-/middle-/short-wavelength sensitive). Phylogenetic analyses indicate these novel crustacean opsins form a monophyletic clade with previously characterized crayfish opsin sequences and form a sister group to insect middle-/long-wavelength-sensitive opsins. The reconstructed opsin phylogeny and the corresponding spectral data for each sequence were used to investigate selective influences within arthropod, and mainly "pancrustacean," opsin evolution using standard dN/dS ratio methods and more sensitive techniques investigating the amino acid property changes resulting from nonsynonymous replacements in a historical (i.e., phylogenetic) context. Although the conservative dN/dS methods did not detect any selection, 4 amino acid properties (coil tendencies, compressibility, power to be at the middle of an alpha-helix, and refractive index) were found to be influenced by destabilizing positive selection. Ten amino acid sites relating to these properties were found to face the binding pocket, within 4 A of the chromophore and thus have the potential to affect spectral tuning.

Authors+Show Affiliations

Department of Microbiology and Molecular Biology, Brigham Young University. porter@umbc.eduNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

17053049

Citation

Porter, Megan L., et al. "Molecular Characterization of Crustacean Visual Pigments and the Evolution of Pancrustacean Opsins." Molecular Biology and Evolution, vol. 24, no. 1, 2007, pp. 253-68.
Porter ML, Cronin TW, McClellan DA, et al. Molecular characterization of crustacean visual pigments and the evolution of pancrustacean opsins. Mol Biol Evol. 2007;24(1):253-68.
Porter, M. L., Cronin, T. W., McClellan, D. A., & Crandall, K. A. (2007). Molecular characterization of crustacean visual pigments and the evolution of pancrustacean opsins. Molecular Biology and Evolution, 24(1), 253-68.
Porter ML, et al. Molecular Characterization of Crustacean Visual Pigments and the Evolution of Pancrustacean Opsins. Mol Biol Evol. 2007;24(1):253-68. PubMed PMID: 17053049.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular characterization of crustacean visual pigments and the evolution of pancrustacean opsins. AU - Porter,Megan L, AU - Cronin,Thomas W, AU - McClellan,David A, AU - Crandall,Keith A, Y1 - 2006/10/19/ PY - 2006/10/21/pubmed PY - 2007/4/3/medline PY - 2006/10/21/entrez SP - 253 EP - 68 JF - Molecular biology and evolution JO - Mol Biol Evol VL - 24 IS - 1 N2 - Investigations of opsin evolution outside of vertebrate systems have long been focused on insect visual pigments, whereas other groups have received little attention. Furthermore, few studies have explicitly investigated the selective influences across all the currently characterized arthropod opsins. In this study, we contribute to the knowledge of crustacean opsins by sequencing 1 opsin gene each from 6 previously uncharacterized crustacean species (Euphausia superba, Homarus gammarus, Archaeomysis grebnitzkii, Holmesimysis costata, Mysis diluviana, and Neomysis americana). Visual pigment spectral absorbances were measured using microspectrophotometry for species not previously characterized (A. grebnitzkii=496 nm, H. costata=512 nm, M. diluviana=501 nm, and N. americana=520 nm). These novel crustacean opsin sequences were included in a phylogenetic analysis with previously characterized arthropod opsin sequences to determine the evolutionary placement relative to the well-established insect spectral clades (long-/middle-/short-wavelength sensitive). Phylogenetic analyses indicate these novel crustacean opsins form a monophyletic clade with previously characterized crayfish opsin sequences and form a sister group to insect middle-/long-wavelength-sensitive opsins. The reconstructed opsin phylogeny and the corresponding spectral data for each sequence were used to investigate selective influences within arthropod, and mainly "pancrustacean," opsin evolution using standard dN/dS ratio methods and more sensitive techniques investigating the amino acid property changes resulting from nonsynonymous replacements in a historical (i.e., phylogenetic) context. Although the conservative dN/dS methods did not detect any selection, 4 amino acid properties (coil tendencies, compressibility, power to be at the middle of an alpha-helix, and refractive index) were found to be influenced by destabilizing positive selection. Ten amino acid sites relating to these properties were found to face the binding pocket, within 4 A of the chromophore and thus have the potential to affect spectral tuning. SN - 0737-4038 UR - https://www.unboundmedicine.com/medline/citation/17053049/Molecular_characterization_of_crustacean_visual_pigments_and_the_evolution_of_pancrustacean_opsins_ L2 - https://academic.oup.com/mbe/article-lookup/doi/10.1093/molbev/msl152 DB - PRIME DP - Unbound Medicine ER -