Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.

Odorant-binding proteins (OBPs) are extracellular proteins found in insect chemosensilla, where they participate in the sensing of odors, tastes, and pheromones. Although a large number of OBP genes have been identified in insect genomes, their molecular functions and biological roles have been clar...

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Autores principales:	Eriko Harada, Jun Nakagawa, Tsunaki Asano, Masato Taoka, Hiroyuki Sorimachi, Yoshihiro Ito, Toshiro Aigaki, Takashi Matsuo
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fbb923d1139246cb83a0269e5c030240
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spelling	oai:doaj.org-article:fbb923d1139246cb83a0269e5c0302402021-11-18T07:30:47ZFunctional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.1932-620310.1371/journal.pone.0029710https://doaj.org/article/fbb923d1139246cb83a0269e5c0302402012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22238638/?tool=EBIhttps://doaj.org/toc/1932-6203Odorant-binding proteins (OBPs) are extracellular proteins found in insect chemosensilla, where they participate in the sensing of odors, tastes, and pheromones. Although a large number of OBP genes have been identified in insect genomes, their molecular functions and biological roles have been clarified in limited cases. Two OBP genes, Obp57d and Obp57e, were involved in the evolution of host-plant preference in Drosophila sechellia. Comparative analyses of the Obp57d/e genomic sequences from 27 closely related species suggested that the two genes arose by tandem gene duplication and functionally diverged from each other. In this study, the functional evolution of Obp57d and Obp57e was examined by in vitro binding assays using recombinant proteins synthesized in a bacterial system. Compared to the ancestral Dpse\OBP57de, Dmel\OBP57d was more specialized to tridecanoic acid while Dmel\OBP57e was generalized regarding their binding affinity, suggesting that the two OBP genes underwent subfunctionalization and neofunctionalization. A behavioral analysis using knockout flies supported that the biological role is different between OBP57d and OBP57e in vivo. Site-directed mutagenesis of the evolutionarily conserved amino acids revealed that these residues play an important role in protein folding. These findings provide a clue to understanding how the repertoire of OBP genes is maintained in a genome under natural selection.Eriko HaradaJun NakagawaTsunaki AsanoMasato TaokaHiroyuki SorimachiYoshihiro ItoToshiro AigakiTakashi MatsuoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 1, p e29710 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Eriko Harada Jun Nakagawa Tsunaki Asano Masato Taoka Hiroyuki Sorimachi Yoshihiro Ito Toshiro Aigaki Takashi Matsuo Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.
description	Odorant-binding proteins (OBPs) are extracellular proteins found in insect chemosensilla, where they participate in the sensing of odors, tastes, and pheromones. Although a large number of OBP genes have been identified in insect genomes, their molecular functions and biological roles have been clarified in limited cases. Two OBP genes, Obp57d and Obp57e, were involved in the evolution of host-plant preference in Drosophila sechellia. Comparative analyses of the Obp57d/e genomic sequences from 27 closely related species suggested that the two genes arose by tandem gene duplication and functionally diverged from each other. In this study, the functional evolution of Obp57d and Obp57e was examined by in vitro binding assays using recombinant proteins synthesized in a bacterial system. Compared to the ancestral Dpse\OBP57de, Dmel\OBP57d was more specialized to tridecanoic acid while Dmel\OBP57e was generalized regarding their binding affinity, suggesting that the two OBP genes underwent subfunctionalization and neofunctionalization. A behavioral analysis using knockout flies supported that the biological role is different between OBP57d and OBP57e in vivo. Site-directed mutagenesis of the evolutionarily conserved amino acids revealed that these residues play an important role in protein folding. These findings provide a clue to understanding how the repertoire of OBP genes is maintained in a genome under natural selection.
format	article
author	Eriko Harada Jun Nakagawa Tsunaki Asano Masato Taoka Hiroyuki Sorimachi Yoshihiro Ito Toshiro Aigaki Takashi Matsuo
author_facet	Eriko Harada Jun Nakagawa Tsunaki Asano Masato Taoka Hiroyuki Sorimachi Yoshihiro Ito Toshiro Aigaki Takashi Matsuo
author_sort	Eriko Harada
title	Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.
title_short	Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.
title_full	Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.
title_fullStr	Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.
title_full_unstemmed	Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.
title_sort	functional evolution of duplicated odorant-binding protein genes, obp57d and obp57e, in drosophila.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/fbb923d1139246cb83a0269e5c030240
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Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila.

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