The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection

The heat-shock protein GroEL is a double-ring-structured chaperonin that assists the folding of many newly synthesized proteins in Escherichia coli and the refolding in vitro, with the cochaperonin GroES, of con damaged proteins. This protein is constitutively overexpressed in the primary symbiotic...

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Autores: Fares, MA, Barrio, E, Sabater-Muñoz, B, Moya, A
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2002
País:España
Institución:Fundación para el Fomento de la Investigación Sanitaria y Biomédica de la Comunitat Valenciana (FISABIO)
Repositorio:r-FISABIO. Repositorio Institucional de Producción Científica
OAI Identifier:oai:fisabio.fundanetsuite.com:p17225
Acceso en línea:https://fisabio.portalinvestigacion.com/publicaciones/17225
Access Level:acceso abierto
Palabra clave:aphid endosymbionts
Buchnera aphidicola
groEL
positive selection
rates of evolution
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spelling The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selectionFares, MABarrio, ESabater-Muñoz, BMoya, Aaphid endosymbiontsBuchnera aphidicolagroELpositive selectionrates of evolutionThe heat-shock protein GroEL is a double-ring-structured chaperonin that assists the folding of many newly synthesized proteins in Escherichia coli and the refolding in vitro, with the cochaperonin GroES, of con damaged proteins. This protein is constitutively overexpressed in the primary symbiotic bacteria of many insects. constituting approximately 10% of the total protein in Buchnera. the primary endosymbiont of aphids. In the present study, we perform a maximum likelihood (ML) analysis to unveil the selective constraints in GroEL. In addition. we apply a new statistical approach to determine the patterns of evolution in this highly interesting protein. The main conclusion derived from our analysis is that GroEL has Suffered an accelerated rate of amino acid Substitution upon the symbiotic integration of Buchnera into the aphids. It is most interesting that the ML analysis of codon substitutions in the different branches of the phylogenetic tree strongly Supports the action of positive selection in the different lineages of Buchnera. Additionally. the new sliding window analysis of the complete groEL sequence reveals different re-ions of the molecule Under the action of positive selection. mainly located in the apical domain, that are important for both peptide and GroES binding.Oxford University Press2002info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://fisabio.portalinvestigacion.com/publicaciones/17225MOLECULAR BIOLOGY AND EVOLUTIONISSN: 15371719ISSNe: 07374038reponame:r-FISABIO. Repositorio Institucional de Producción Científicainstname:Fundación para el Fomento de la Investigación Sanitaria y Biomédica de la Comunitat Valenciana (FISABIO)Inglésinfo:eu-repo/semantics/openAccessoai:fisabio.fundanetsuite.com:p172252026-06-11T12:45:17Z
dc.title.none.fl_str_mv The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
title The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
spellingShingle The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
Fares, MA
aphid endosymbionts
Buchnera aphidicola
groEL
positive selection
rates of evolution
title_short The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
title_full The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
title_fullStr The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
title_full_unstemmed The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
title_sort The evolution of the heat-shock protein GroEL from <i>Buchnera</i>, the primary endosymbiont of aphids, is governed by positive selection
dc.creator.none.fl_str_mv Fares, MA
Barrio, E
Sabater-Muñoz, B
Moya, A
author Fares, MA
author_facet Fares, MA
Barrio, E
Sabater-Muñoz, B
Moya, A
author_role author
author2 Barrio, E
Sabater-Muñoz, B
Moya, A
author2_role author
author
author
dc.subject.none.fl_str_mv aphid endosymbionts
Buchnera aphidicola
groEL
positive selection
rates of evolution
topic aphid endosymbionts
Buchnera aphidicola
groEL
positive selection
rates of evolution
description The heat-shock protein GroEL is a double-ring-structured chaperonin that assists the folding of many newly synthesized proteins in Escherichia coli and the refolding in vitro, with the cochaperonin GroES, of con damaged proteins. This protein is constitutively overexpressed in the primary symbiotic bacteria of many insects. constituting approximately 10% of the total protein in Buchnera. the primary endosymbiont of aphids. In the present study, we perform a maximum likelihood (ML) analysis to unveil the selective constraints in GroEL. In addition. we apply a new statistical approach to determine the patterns of evolution in this highly interesting protein. The main conclusion derived from our analysis is that GroEL has Suffered an accelerated rate of amino acid Substitution upon the symbiotic integration of Buchnera into the aphids. It is most interesting that the ML analysis of codon substitutions in the different branches of the phylogenetic tree strongly Supports the action of positive selection in the different lineages of Buchnera. Additionally. the new sliding window analysis of the complete groEL sequence reveals different re-ions of the molecule Under the action of positive selection. mainly located in the apical domain, that are important for both peptide and GroES binding.
publishDate 2002
dc.date.none.fl_str_mv 2002
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://fisabio.portalinvestigacion.com/publicaciones/17225
url https://fisabio.portalinvestigacion.com/publicaciones/17225
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv MOLECULAR BIOLOGY AND EVOLUTION
ISSN: 15371719
ISSNe: 07374038
reponame:r-FISABIO. Repositorio Institucional de Producción Científica
instname:Fundación para el Fomento de la Investigación Sanitaria y Biomédica de la Comunitat Valenciana (FISABIO)
instname_str Fundación para el Fomento de la Investigación Sanitaria y Biomédica de la Comunitat Valenciana (FISABIO)
reponame_str r-FISABIO. Repositorio Institucional de Producción Científica
collection r-FISABIO. Repositorio Institucional de Producción Científica
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.812455

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