Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi

Autores
Avila, Maria Lara; Bercovich, Natalia; Westergaard, Gaston; Levin, Mariano Jorge; Vazquez, Martin Pablo
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
SF3b155 and p14 are essential components of spliceosome core that recognize the branch point adenosine, a critical step in splicing in eukaryotes. Trypanosomes are unusual since every transcribed gene is processed by trans-splicing instead of cis-splicing. Thus, the trans-spliceosome emerges as an interesting anti-parasitic drug target since this process is not present in mammalian hosts. Here, we present the orthologues of these proteins in Trypanosoma cruzi that interact strongly with each other. To define similarities and differences with the human pair, we performed a detailed alanine scan analysis that allowed us to identify the regions and the critical amino acids of T. cruzi SF3b155 involved in interaction with p14. We demonstrate that the T. cruzi SF3b155 interface is larger and contains more complex elements than its human counterpart. Additionally, our results provide the first insights into the core of the putative mRNA processing complex of trypanosomes.
Fil: Avila, Maria Lara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Bercovich, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Westergaard, Gaston. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Levin, Mariano Jorge. Institut Cochin; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vazquez, Martin Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Materia
Drug Targets
Protein Interaction
Trans-Splicing
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:11336/79673
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79673
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruziAvila, Maria LaraBercovich, NataliaWestergaard, GastonLevin, Mariano JorgeVazquez, Martin PabloDrug TargetsProtein InteractionTrans-Splicinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1SF3b155 and p14 are essential components of spliceosome core that recognize the branch point adenosine, a critical step in splicing in eukaryotes. Trypanosomes are unusual since every transcribed gene is processed by trans-splicing instead of cis-splicing. Thus, the trans-spliceosome emerges as an interesting anti-parasitic drug target since this process is not present in mammalian hosts. Here, we present the orthologues of these proteins in Trypanosoma cruzi that interact strongly with each other. To define similarities and differences with the human pair, we performed a detailed alanine scan analysis that allowed us to identify the regions and the critical amino acids of T. cruzi SF3b155 involved in interaction with p14. We demonstrate that the T. cruzi SF3b155 interface is larger and contains more complex elements than its human counterpart. Additionally, our results provide the first insights into the core of the putative mRNA processing complex of trypanosomes.Fil: Avila, Maria Lara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Bercovich, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Westergaard, Gaston. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Levin, Mariano Jorge. Institut Cochin; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Vazquez, Martin Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaAcademic Press Inc Elsevier Science2007-12info: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/11336/79673Avila, Maria Lara; Bercovich, Natalia; Westergaard, Gaston; Levin, Mariano Jorge; Vazquez, Martin Pablo; Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 364; 1; 12-2007; 26-320006-291XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2007.09.090info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006291X07020815info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:40:55Zoai:ri.conicet.gov.ar:11336/79673instacron: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 09:40:55.494CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
title Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
spellingShingle Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
Avila, Maria Lara
Drug Targets
Protein Interaction
Trans-Splicing
title_short Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
title_full Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
title_fullStr Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
title_full_unstemmed Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
title_sort Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi
dc.creator.none.fl_str_mv Avila, Maria Lara
Bercovich, Natalia
Westergaard, Gaston
Levin, Mariano Jorge
Vazquez, Martin Pablo
author Avila, Maria Lara
author_facet Avila, Maria Lara
Bercovich, Natalia
Westergaard, Gaston
Levin, Mariano Jorge
Vazquez, Martin Pablo
author_role author
author2 Bercovich, Natalia
Westergaard, Gaston
Levin, Mariano Jorge
Vazquez, Martin Pablo
author2_role author
author
author
author
dc.subject.none.fl_str_mv Drug Targets
Protein Interaction
Trans-Splicing
topic Drug Targets
Protein Interaction
Trans-Splicing
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv SF3b155 and p14 are essential components of spliceosome core that recognize the branch point adenosine, a critical step in splicing in eukaryotes. Trypanosomes are unusual since every transcribed gene is processed by trans-splicing instead of cis-splicing. Thus, the trans-spliceosome emerges as an interesting anti-parasitic drug target since this process is not present in mammalian hosts. Here, we present the orthologues of these proteins in Trypanosoma cruzi that interact strongly with each other. To define similarities and differences with the human pair, we performed a detailed alanine scan analysis that allowed us to identify the regions and the critical amino acids of T. cruzi SF3b155 involved in interaction with p14. We demonstrate that the T. cruzi SF3b155 interface is larger and contains more complex elements than its human counterpart. Additionally, our results provide the first insights into the core of the putative mRNA processing complex of trypanosomes.
Fil: Avila, Maria Lara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Bercovich, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Westergaard, Gaston. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Levin, Mariano Jorge. Institut Cochin; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vazquez, Martin Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
description SF3b155 and p14 are essential components of spliceosome core that recognize the branch point adenosine, a critical step in splicing in eukaryotes. Trypanosomes are unusual since every transcribed gene is processed by trans-splicing instead of cis-splicing. Thus, the trans-spliceosome emerges as an interesting anti-parasitic drug target since this process is not present in mammalian hosts. Here, we present the orthologues of these proteins in Trypanosoma cruzi that interact strongly with each other. To define similarities and differences with the human pair, we performed a detailed alanine scan analysis that allowed us to identify the regions and the critical amino acids of T. cruzi SF3b155 involved in interaction with p14. We demonstrate that the T. cruzi SF3b155 interface is larger and contains more complex elements than its human counterpart. Additionally, our results provide the first insights into the core of the putative mRNA processing complex of trypanosomes.
publishDate 2007
dc.date.none.fl_str_mv 2007-12
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/11336/79673
Avila, Maria Lara; Bercovich, Natalia; Westergaard, Gaston; Levin, Mariano Jorge; Vazquez, Martin Pablo; Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 364; 1; 12-2007; 26-32
0006-291X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79673
identifier_str_mv Avila, Maria Lara; Bercovich, Natalia; Westergaard, Gaston; Levin, Mariano Jorge; Vazquez, Martin Pablo; Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 364; 1; 12-2007; 26-32
0006-291X
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.bbrc.2007.09.090
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006291X07020815
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
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
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_ 1844613294895136768
score 13.070432

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