Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity

Olfactory receptor repertoires exhibit remarkable functional diversity, but how these proteins have evolved is poorly understood. Through analysis of extant and ancestrally reconstructed drosophilid olfactory receptors from the Ionotropic receptor (Ir) family, we investigated evolution of two organi...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Lucia L Prieto-Godino, Hayden R Schmidt, Richard Benton
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	olfactory receptor Drosophila sechellia mutation parallel evolution ligand-binding neurophysiology Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/98c1051c69b24dbeb775d0fbe1642234
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:98c1051c69b24dbeb775d0fbe1642234
record_format	dspace
spelling	oai:doaj.org-article:98c1051c69b24dbeb775d0fbe16422342021-11-24T12:31:50ZMolecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity10.7554/eLife.697322050-084Xe69732https://doaj.org/article/98c1051c69b24dbeb775d0fbe16422342021-10-01T00:00:00Zhttps://elifesciences.org/articles/69732https://doaj.org/toc/2050-084XOlfactory receptor repertoires exhibit remarkable functional diversity, but how these proteins have evolved is poorly understood. Through analysis of extant and ancestrally reconstructed drosophilid olfactory receptors from the Ionotropic receptor (Ir) family, we investigated evolution of two organic acid-sensing receptors, Ir75a and Ir75b. Despite their low amino acid identity, we identify a common ‘hotspot’ in their ligand-binding pocket that has a major effect on changing the specificity of both Irs, as well as at least two distinct functional transitions in Ir75a during evolution. Moreover, we show that odor specificity is refined by changes in additional, receptor-specific sites, including those outside the ligand-binding pocket. Our work reveals how a core, common determinant of ligand-tuning acts within epistatic and allosteric networks of substitutions to lead to functional evolution of olfactory receptors.Lucia L Prieto-GodinoHayden R SchmidtRichard BentoneLife Sciences Publications Ltdarticleolfactory receptorDrosophila sechelliamutationparallel evolutionligand-bindingneurophysiologyMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	olfactory receptor Drosophila sechellia mutation parallel evolution ligand-binding neurophysiology Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	olfactory receptor Drosophila sechellia mutation parallel evolution ligand-binding neurophysiology Medicine R Science Q Biology (General) QH301-705.5 Lucia L Prieto-Godino Hayden R Schmidt Richard Benton Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
description	Olfactory receptor repertoires exhibit remarkable functional diversity, but how these proteins have evolved is poorly understood. Through analysis of extant and ancestrally reconstructed drosophilid olfactory receptors from the Ionotropic receptor (Ir) family, we investigated evolution of two organic acid-sensing receptors, Ir75a and Ir75b. Despite their low amino acid identity, we identify a common ‘hotspot’ in their ligand-binding pocket that has a major effect on changing the specificity of both Irs, as well as at least two distinct functional transitions in Ir75a during evolution. Moreover, we show that odor specificity is refined by changes in additional, receptor-specific sites, including those outside the ligand-binding pocket. Our work reveals how a core, common determinant of ligand-tuning acts within epistatic and allosteric networks of substitutions to lead to functional evolution of olfactory receptors.
format	article
author	Lucia L Prieto-Godino Hayden R Schmidt Richard Benton
author_facet	Lucia L Prieto-Godino Hayden R Schmidt Richard Benton
author_sort	Lucia L Prieto-Godino
title	Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
title_short	Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
title_full	Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
title_fullStr	Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
title_full_unstemmed	Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
title_sort	molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/98c1051c69b24dbeb775d0fbe1642234
work_keys_str_mv	AT lucialprietogodino molecularreconstructionofrecurrentevolutionaryswitchinginolfactoryreceptorspecificity AT haydenrschmidt molecularreconstructionofrecurrentevolutionaryswitchinginolfactoryreceptorspecificity AT richardbenton molecularreconstructionofrecurrentevolutionaryswitchinginolfactoryreceptorspecificity
_version_	1718415062160375808

Molecular reconstruction of recurrent evolutionary switching in olfactory receptor specificity

Ejemplares similares