Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns

Autores
Palopoli, Nicolás; Marchetti, Julia; Monzon, Alexander M.; Zea, Diego J.; Tosatto, Silvio C.E.; Fornasari, Maria Silvina; Parisi, Gustavo Daniel
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using NMR ensembles, we found that IDPs evolve under a strong site-specific evolutionary rate heterogeneity, mainly originated by different constraints derived from their inter-residue contacts. Evolutionary rate profiles correlate with the experimentally observed conformational diversity of the protein, allowing the description of different conformational patterns possibly related to their structure-function relationships. The correlation between evolutionary rates and contact information improves when structural information is taken not from any individual conformer or the whole ensemble, but from combining a limited number of conformers. Our results suggest that residue contacts in disordered regions constrain evolutionary rates to conserve the dynamic behaviour of the ensemble and that evolutionary rates can be used as a proxy for the conformational diversity of IDPs.
Fil: Palopoli, Nicolás. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Monzon, Alexander M.. Università di Padova; Italia
Fil: Zea, Diego J.. Sorbonne University; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Tosatto, Silvio C.E.. Università di Padova; Italia
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
CONFORMATIONAL DIVERSITY
EVOLUTIONARY RATES
INTRINSIC DISORDER
PROTEIN ENSEMBLES
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/153567
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational PatternsPalopoli, NicolásMarchetti, JuliaMonzon, Alexander M.Zea, Diego J.Tosatto, Silvio C.E.Fornasari, Maria SilvinaParisi, Gustavo DanielCONFORMATIONAL DIVERSITYEVOLUTIONARY RATESINTRINSIC DISORDERPROTEIN ENSEMBLEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using NMR ensembles, we found that IDPs evolve under a strong site-specific evolutionary rate heterogeneity, mainly originated by different constraints derived from their inter-residue contacts. Evolutionary rate profiles correlate with the experimentally observed conformational diversity of the protein, allowing the description of different conformational patterns possibly related to their structure-function relationships. The correlation between evolutionary rates and contact information improves when structural information is taken not from any individual conformer or the whole ensemble, but from combining a limited number of conformers. Our results suggest that residue contacts in disordered regions constrain evolutionary rates to conserve the dynamic behaviour of the ensemble and that evolutionary rates can be used as a proxy for the conformational diversity of IDPs.Fil: Palopoli, Nicolás. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Monzon, Alexander M.. Università di Padova; ItaliaFil: Zea, Diego J.. Sorbonne University; Francia. Centre National de la Recherche Scientifique; FranciaFil: Tosatto, Silvio C.E.. Università di Padova; ItaliaFil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAcademic Press Ltd - Elsevier Science Ltd2021-02-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/153567Palopoli, Nicolás; Marchetti, Julia; Monzon, Alexander M.; Zea, Diego J.; Tosatto, Silvio C.E.; et al.; Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 433; 3; 5-2-2021; 1-120022-28361089-8638CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022283620306768info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2020.166751info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:47:33Zoai:ri.conicet.gov.ar:11336/153567instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:47:33.545CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
title Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
spellingShingle Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
Palopoli, Nicolás
CONFORMATIONAL DIVERSITY
EVOLUTIONARY RATES
INTRINSIC DISORDER
PROTEIN ENSEMBLES
title_short Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
title_full Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
title_fullStr Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
title_full_unstemmed Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
title_sort Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns
dc.creator.none.fl_str_mv Palopoli, Nicolás
Marchetti, Julia
Monzon, Alexander M.
Zea, Diego J.
Tosatto, Silvio C.E.
Fornasari, Maria Silvina
Parisi, Gustavo Daniel
author Palopoli, Nicolás
author_facet Palopoli, Nicolás
Marchetti, Julia
Monzon, Alexander M.
Zea, Diego J.
Tosatto, Silvio C.E.
Fornasari, Maria Silvina
Parisi, Gustavo Daniel
author_role author
author2 Marchetti, Julia
Monzon, Alexander M.
Zea, Diego J.
Tosatto, Silvio C.E.
Fornasari, Maria Silvina
Parisi, Gustavo Daniel
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv CONFORMATIONAL DIVERSITY
EVOLUTIONARY RATES
INTRINSIC DISORDER
PROTEIN ENSEMBLES
topic CONFORMATIONAL DIVERSITY
EVOLUTIONARY RATES
INTRINSIC DISORDER
PROTEIN ENSEMBLES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using NMR ensembles, we found that IDPs evolve under a strong site-specific evolutionary rate heterogeneity, mainly originated by different constraints derived from their inter-residue contacts. Evolutionary rate profiles correlate with the experimentally observed conformational diversity of the protein, allowing the description of different conformational patterns possibly related to their structure-function relationships. The correlation between evolutionary rates and contact information improves when structural information is taken not from any individual conformer or the whole ensemble, but from combining a limited number of conformers. Our results suggest that residue contacts in disordered regions constrain evolutionary rates to conserve the dynamic behaviour of the ensemble and that evolutionary rates can be used as a proxy for the conformational diversity of IDPs.
Fil: Palopoli, Nicolás. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Monzon, Alexander M.. Università di Padova; Italia
Fil: Zea, Diego J.. Sorbonne University; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Tosatto, Silvio C.E.. Università di Padova; Italia
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using NMR ensembles, we found that IDPs evolve under a strong site-specific evolutionary rate heterogeneity, mainly originated by different constraints derived from their inter-residue contacts. Evolutionary rate profiles correlate with the experimentally observed conformational diversity of the protein, allowing the description of different conformational patterns possibly related to their structure-function relationships. The correlation between evolutionary rates and contact information improves when structural information is taken not from any individual conformer or the whole ensemble, but from combining a limited number of conformers. Our results suggest that residue contacts in disordered regions constrain evolutionary rates to conserve the dynamic behaviour of the ensemble and that evolutionary rates can be used as a proxy for the conformational diversity of IDPs.
publishDate 2021
dc.date.none.fl_str_mv 2021-02-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/153567
Palopoli, Nicolás; Marchetti, Julia; Monzon, Alexander M.; Zea, Diego J.; Tosatto, Silvio C.E.; et al.; Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 433; 3; 5-2-2021; 1-12
0022-2836
1089-8638
CONICET Digital
CONICET
url http://hdl.handle.net/11336/153567
identifier_str_mv Palopoli, Nicolás; Marchetti, Julia; Monzon, Alexander M.; Zea, Diego J.; Tosatto, Silvio C.E.; et al.; Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 433; 3; 5-2-2021; 1-12
0022-2836
1089-8638
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022283620306768
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2020.166751
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Ltd - Elsevier Science Ltd
publisher.none.fl_str_mv Academic Press Ltd - Elsevier Science Ltd
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613481673785344
score 13.070432

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