Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution

Autores
Marchetti, Julia; Monzón, Alexander; Tosatto, Silvio C.E.; Parisi, Gustavo Daniel; Fornasari, Maria Silvina
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The conformations accessible to proteins are determined by the inter-residue interactions between amino acid residues. During evolution, structural constraints that are required for protein function providing biologically relevant information can exist. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered and disordered proteins. Using a structurally constrained model of protein evolution, we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~ 68% are in disordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~ 11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles.
Fil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Università di Padova; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tosatto, Silvio C.E.. Università di Padova; Italia
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
CONFORMATIONAL DIVERSITY
DISORDERED PROTEINS
PROTEIN ENSEMBLE
PROTEIN EVOLUTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/133240
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during EvolutionMarchetti, JuliaMonzón, AlexanderTosatto, Silvio C.E.Parisi, Gustavo DanielFornasari, Maria SilvinaCONFORMATIONAL DIVERSITYDISORDERED PROTEINSPROTEIN ENSEMBLEPROTEIN EVOLUTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The conformations accessible to proteins are determined by the inter-residue interactions between amino acid residues. During evolution, structural constraints that are required for protein function providing biologically relevant information can exist. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered and disordered proteins. Using a structurally constrained model of protein evolution, we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~ 68% are in disordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~ 11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles.Fil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Università di Padova; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Tosatto, Silvio C.E.. Università di Padova; ItaliaFil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAcademic Press Ltd - Elsevier Science Ltd2019-03-15info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/133240Marchetti, Julia; Monzón, Alexander; Tosatto, Silvio C.E.; Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 431; 6; 15-3-2019; 1298-13070022-2836CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2019.01.031info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0022283619300488info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-17T11:19:15Zoai:ri.conicet.gov.ar:11336/133240instacron: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:34982025-09-17 11:19:15.287CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
title Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
spellingShingle Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
Marchetti, Julia
CONFORMATIONAL DIVERSITY
DISORDERED PROTEINS
PROTEIN ENSEMBLE
PROTEIN EVOLUTION
title_short Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
title_full Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
title_fullStr Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
title_full_unstemmed Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
title_sort Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
dc.creator.none.fl_str_mv Marchetti, Julia
Monzón, Alexander
Tosatto, Silvio C.E.
Parisi, Gustavo Daniel
Fornasari, Maria Silvina
author Marchetti, Julia
author_facet Marchetti, Julia
Monzón, Alexander
Tosatto, Silvio C.E.
Parisi, Gustavo Daniel
Fornasari, Maria Silvina
author_role author
author2 Monzón, Alexander
Tosatto, Silvio C.E.
Parisi, Gustavo Daniel
Fornasari, Maria Silvina
author2_role author
author
author
author
dc.subject.none.fl_str_mv CONFORMATIONAL DIVERSITY
DISORDERED PROTEINS
PROTEIN ENSEMBLE
PROTEIN EVOLUTION
topic CONFORMATIONAL DIVERSITY
DISORDERED PROTEINS
PROTEIN ENSEMBLE
PROTEIN EVOLUTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The conformations accessible to proteins are determined by the inter-residue interactions between amino acid residues. During evolution, structural constraints that are required for protein function providing biologically relevant information can exist. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered and disordered proteins. Using a structurally constrained model of protein evolution, we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~ 68% are in disordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~ 11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles.
Fil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Università di Padova; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tosatto, Silvio C.E.. Università di Padova; Italia
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The conformations accessible to proteins are determined by the inter-residue interactions between amino acid residues. During evolution, structural constraints that are required for protein function providing biologically relevant information can exist. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered and disordered proteins. Using a structurally constrained model of protein evolution, we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~ 68% are in disordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~ 11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles.
publishDate 2019
dc.date.none.fl_str_mv 2019-03-15
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/11336/133240
Marchetti, Julia; Monzón, Alexander; Tosatto, Silvio C.E.; Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 431; 6; 15-3-2019; 1298-1307
0022-2836
CONICET Digital
CONICET
url http://hdl.handle.net/11336/133240
identifier_str_mv Marchetti, Julia; Monzón, Alexander; Tosatto, Silvio C.E.; Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 431; 6; 15-3-2019; 1298-1307
0022-2836
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2019.01.031
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0022283619300488
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
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
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score 13.000565

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