Structured Tandem Repeats in Protein Interactions

Autores
Mac Donagh, Juan; Marchesini, Abril; Spiga, Agostina; Fallico, Maximiliano José; Arrias, Paula Nazarena; Monzon, Alexander Miguel; Vagiona, Aimilia Christina; Gonçalves Kulik, Mariane; Mier, Pablo; Andrade Navarro, Miguel A.
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Tandem repeats (TRs) in protein sequences are consecutive, highly similar sequence motifs. Some types of TRs fold into structural units that pack together in ensembles, forming either an (open) elongated domain or a (closed) propeller, where the last unit of the ensemble packs against the first one. Here, we examine TR proteins (TRPs) to see how their sequence, structure, and evolutionary properties favor them for a function as mediators of protein interactions. Our observations suggest that TRPs bind other proteins using large, structured surfaces like globular domains; in particular, open-structured TR ensembles are favored by flexible termini and the possibility to tightly coil against their targets. While, intuitively, open ensembles of TRs seem prone to evolve due to their potential to accommodate insertions and deletions of units, these evolutionary events are unexpectedly rare, suggesting that they are advantageous for the emergence of the ancestral sequence but are early fixed. We hypothesize that their flexibility makes it easier for further proteins to adapt to interact with them, which would explain their large number of protein interactions. We provide insight into the properties of open TR ensembles, which make them scaffolds for alternative protein complexes to organize genes, RNA and proteins.
Fil: Mac Donagh, Juan. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marchesini, Abril. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Spiga, Agostina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Fallico, Maximiliano José. Universidad Nacional de La Plata. Facultad de Ciencas Exactas. Laboratorio de Investigación y Desarrollo de Bioactivos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Arrias, Paula Nazarena. Università di Padova; Italia
Fil: Monzon, Alexander Miguel. Dipartamento Di Ingegneria Dell' Informazione ; Universita Degli Studi Di Padova;
Fil: Vagiona, Aimilia Christina. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Gonçalves Kulik, Mariane. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Mier, Pablo. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Andrade Navarro, Miguel A.. Johannes Gutenberg Universitat Mainz; Alemania
Materia
TANDEM REPEAT
PROTEIN-PROTEIN INTERACTIONS
PROTEIN STRUCTURE
PROTEIN EVOLUTION
PROTEIN FLEXIBILITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/231736
Acceder
id CONICETDig_428961568344fda83afa4176bf3c8762
oai_identifier_str oai:ri.conicet.gov.ar:11336/231736
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structured Tandem Repeats in Protein InteractionsMac Donagh, JuanMarchesini, AbrilSpiga, AgostinaFallico, Maximiliano JoséArrias, Paula NazarenaMonzon, Alexander MiguelVagiona, Aimilia ChristinaGonçalves Kulik, MarianeMier, PabloAndrade Navarro, Miguel A.TANDEM REPEATPROTEIN-PROTEIN INTERACTIONSPROTEIN STRUCTUREPROTEIN EVOLUTIONPROTEIN FLEXIBILITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Tandem repeats (TRs) in protein sequences are consecutive, highly similar sequence motifs. Some types of TRs fold into structural units that pack together in ensembles, forming either an (open) elongated domain or a (closed) propeller, where the last unit of the ensemble packs against the first one. Here, we examine TR proteins (TRPs) to see how their sequence, structure, and evolutionary properties favor them for a function as mediators of protein interactions. Our observations suggest that TRPs bind other proteins using large, structured surfaces like globular domains; in particular, open-structured TR ensembles are favored by flexible termini and the possibility to tightly coil against their targets. While, intuitively, open ensembles of TRs seem prone to evolve due to their potential to accommodate insertions and deletions of units, these evolutionary events are unexpectedly rare, suggesting that they are advantageous for the emergence of the ancestral sequence but are early fixed. We hypothesize that their flexibility makes it easier for further proteins to adapt to interact with them, which would explain their large number of protein interactions. We provide insight into the properties of open TR ensembles, which make them scaffolds for alternative protein complexes to organize genes, RNA and proteins.Fil: Mac Donagh, Juan. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marchesini, Abril. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Spiga, Agostina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Fallico, Maximiliano José. Universidad Nacional de La Plata. Facultad de Ciencas Exactas. Laboratorio de Investigación y Desarrollo de Bioactivos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Arrias, Paula Nazarena. Università di Padova; ItaliaFil: Monzon, Alexander Miguel. Dipartamento Di Ingegneria Dell' Informazione ; Universita Degli Studi Di Padova;Fil: Vagiona, Aimilia Christina. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Gonçalves Kulik, Mariane. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Mier, Pablo. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Andrade Navarro, Miguel A.. Johannes Gutenberg Universitat Mainz; AlemaniaMolecular Diversity Preservation International2024-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/231736Mac Donagh, Juan; Marchesini, Abril; Spiga, Agostina; Fallico, Maximiliano José; Arrias, Paula Nazarena; et al.; Structured Tandem Repeats in Protein Interactions; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 25; 5; 3-2024; 1-111422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms25052994info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:15:33Zoai:ri.conicet.gov.ar:11336/231736instacron: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:34982025-10-15 15:15:33.484CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structured Tandem Repeats in Protein Interactions
title Structured Tandem Repeats in Protein Interactions
spellingShingle Structured Tandem Repeats in Protein Interactions
Mac Donagh, Juan
TANDEM REPEAT
PROTEIN-PROTEIN INTERACTIONS
PROTEIN STRUCTURE
PROTEIN EVOLUTION
PROTEIN FLEXIBILITY
title_short Structured Tandem Repeats in Protein Interactions
title_full Structured Tandem Repeats in Protein Interactions
title_fullStr Structured Tandem Repeats in Protein Interactions
title_full_unstemmed Structured Tandem Repeats in Protein Interactions
title_sort Structured Tandem Repeats in Protein Interactions
dc.creator.none.fl_str_mv Mac Donagh, Juan
Marchesini, Abril
Spiga, Agostina
Fallico, Maximiliano José
Arrias, Paula Nazarena
Monzon, Alexander Miguel
Vagiona, Aimilia Christina
Gonçalves Kulik, Mariane
Mier, Pablo
Andrade Navarro, Miguel A.
author Mac Donagh, Juan
author_facet Mac Donagh, Juan
Marchesini, Abril
Spiga, Agostina
Fallico, Maximiliano José
Arrias, Paula Nazarena
Monzon, Alexander Miguel
Vagiona, Aimilia Christina
Gonçalves Kulik, Mariane
Mier, Pablo
Andrade Navarro, Miguel A.
author_role author
author2 Marchesini, Abril
Spiga, Agostina
Fallico, Maximiliano José
Arrias, Paula Nazarena
Monzon, Alexander Miguel
Vagiona, Aimilia Christina
Gonçalves Kulik, Mariane
Mier, Pablo
Andrade Navarro, Miguel A.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv TANDEM REPEAT
PROTEIN-PROTEIN INTERACTIONS
PROTEIN STRUCTURE
PROTEIN EVOLUTION
PROTEIN FLEXIBILITY
topic TANDEM REPEAT
PROTEIN-PROTEIN INTERACTIONS
PROTEIN STRUCTURE
PROTEIN EVOLUTION
PROTEIN FLEXIBILITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Tandem repeats (TRs) in protein sequences are consecutive, highly similar sequence motifs. Some types of TRs fold into structural units that pack together in ensembles, forming either an (open) elongated domain or a (closed) propeller, where the last unit of the ensemble packs against the first one. Here, we examine TR proteins (TRPs) to see how their sequence, structure, and evolutionary properties favor them for a function as mediators of protein interactions. Our observations suggest that TRPs bind other proteins using large, structured surfaces like globular domains; in particular, open-structured TR ensembles are favored by flexible termini and the possibility to tightly coil against their targets. While, intuitively, open ensembles of TRs seem prone to evolve due to their potential to accommodate insertions and deletions of units, these evolutionary events are unexpectedly rare, suggesting that they are advantageous for the emergence of the ancestral sequence but are early fixed. We hypothesize that their flexibility makes it easier for further proteins to adapt to interact with them, which would explain their large number of protein interactions. We provide insight into the properties of open TR ensembles, which make them scaffolds for alternative protein complexes to organize genes, RNA and proteins.
Fil: Mac Donagh, Juan. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marchesini, Abril. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Spiga, Agostina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Fallico, Maximiliano José. Universidad Nacional de La Plata. Facultad de Ciencas Exactas. Laboratorio de Investigación y Desarrollo de Bioactivos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Arrias, Paula Nazarena. Università di Padova; Italia
Fil: Monzon, Alexander Miguel. Dipartamento Di Ingegneria Dell' Informazione ; Universita Degli Studi Di Padova;
Fil: Vagiona, Aimilia Christina. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Gonçalves Kulik, Mariane. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Mier, Pablo. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Andrade Navarro, Miguel A.. Johannes Gutenberg Universitat Mainz; Alemania
description Tandem repeats (TRs) in protein sequences are consecutive, highly similar sequence motifs. Some types of TRs fold into structural units that pack together in ensembles, forming either an (open) elongated domain or a (closed) propeller, where the last unit of the ensemble packs against the first one. Here, we examine TR proteins (TRPs) to see how their sequence, structure, and evolutionary properties favor them for a function as mediators of protein interactions. Our observations suggest that TRPs bind other proteins using large, structured surfaces like globular domains; in particular, open-structured TR ensembles are favored by flexible termini and the possibility to tightly coil against their targets. While, intuitively, open ensembles of TRs seem prone to evolve due to their potential to accommodate insertions and deletions of units, these evolutionary events are unexpectedly rare, suggesting that they are advantageous for the emergence of the ancestral sequence but are early fixed. We hypothesize that their flexibility makes it easier for further proteins to adapt to interact with them, which would explain their large number of protein interactions. We provide insight into the properties of open TR ensembles, which make them scaffolds for alternative protein complexes to organize genes, RNA and proteins.
publishDate 2024
dc.date.none.fl_str_mv 2024-03
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/11336/231736
Mac Donagh, Juan; Marchesini, Abril; Spiga, Agostina; Fallico, Maximiliano José; Arrias, Paula Nazarena; et al.; Structured Tandem Repeats in Protein Interactions; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 25; 5; 3-2024; 1-11
1422-0067
CONICET Digital
CONICET
url http://hdl.handle.net/11336/231736
identifier_str_mv Mac Donagh, Juan; Marchesini, Abril; Spiga, Agostina; Fallico, Maximiliano José; Arrias, Paula Nazarena; et al.; Structured Tandem Repeats in Protein Interactions; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 25; 5; 3-2024; 1-11
1422-0067
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms25052994
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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 13.22299

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