Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
Texto Completo: | https://www.arca.fiocruz.br/handle/icict/56114 |
Resumo: | Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil. / Universidade Federal de Pernambuco. Departamento de Genética. Recife, PE, Brasil. |
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Bezerra, Maria J. R.Moura, Danielle M. N.Freire, Eden R.Holetz, Fabíola BarbieriReis, Christian R. S.Monteiro, Tallyta T. S.Pinto, Adriana R. S. PintoZhang, NingRezende, Antonio M.Pereira-Neves, AntonioFigueiredo, Regina C. B. Q.Clayton, ChristineField, Mark C.Carrington, MarkMelo Neto, Osvaldo P. de2022-12-21T15:45:04Z2022-12-21T15:45:04Z2022BEZERRA, Maria J. R. et al. Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei. Front. Mol. Biosci, v. 9, n. 971811, p. 1–22, 2022.2296-889Xhttps://www.arca.fiocruz.br/handle/icict/56114porFrontiers MediaEIF4EEIF4GmRNAProtein BiosynthesisPeptide Chain Initiation, TranslationalEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GBiosíntesis de ProteínasIniciación de la Cadena Peptídica TraduccionalFactor 4E Eucariótico de IniciaciónFactor 4G Eucariótico de IniciaciónBiosynthèse des protéinesInitiation de la traductionFacteur-4E d'initiation eucaryoteFacteur-4G d'initiation eucaryoteBiossíntese de ProteínasIniciação Traducional da Cadeia PeptídicaFator de Iniciação 4E em EucariotosFator de Iniciação 4G em EucariotosTrypanosomaDistinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma bruceiinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleFundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil. / Universidade Federal de Pernambuco. Departamento de Genética. Recife, PE, Brasil.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.School of Life Sciences. University of Dundee. Dundee, Scotland, UK.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Heidelberg University Center for Molecular Biology. Heidelberg, Germany.School of Life Sciences. University of Dundee. Dundee, Scotland, UK. / Institute of Parasitology. Biology Center. Czech Academy of Sciences. České Budějovice, Czech Republic.Department of Biochemistry. University of Cambridge. Cambridge, United Kingdom.Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil.Gene expression in pathogenic protozoans of the family Trypanosomatidae has several novel features, including multiple eIF4F-like complexes involved in protein synthesis. The eukaryotic eIF4F complex, formed mainly by eIF4E and eIF4G subunits, is responsible for the canonical selection of mRNAs required for the initiation of mRNA translation. The best-known complexes implicated in translation in trypanosomatids are based on two related pairs of eIF4E and eIF4G subunits (EIF4E3/EIF4G4 and EIF4E4/EIF4G3), whose functional distinctions remain to be fully described. Here, to define interactomes associated with both complexes in Trypanosoma brucei procyclic forms, we performed parallel immunoprecipitation experiments followed by identification of proteins co-precipitated with the four tagged eIF4E and eIF4G subunits. A number of different protein partners, including RNA binding proteins and helicases, specifically co-precipitate with each complex. Highlights with the EIF4E4/EIF4G3 pair include RBP23, PABP1, EIF4AI and the CRK1 kinase. Co-precipitated partners with the EIF4E3/EIF4G4 pair are more diverse and include DRBD2, PABP2 and different zinc-finger proteins and RNA helicases. EIF4E3/EIF4G4 are essential for viability and to better define their role, we further investigated their phenotypes after knockdown. Depletion of either EIF4E3/EIF4G4 mRNAs lead to aberrant morphology with a more direct impact on events associated with cytokinesis. We also sought to identify those mRNAs differentially associated with each complex through CLIP-seq with the two eIF4E subunits. Predominant among EIF4E4-bound transcripts are those encoding ribosomal proteins, absent from those found with EIF4E3, which are generally more diverse. RNAi mediated depletion of EIF4E4, which does not affect proliferation, does not lead to changes in mRNAs or proteins associated with EIF4E3, confirming a lack of redundancy and distinct roles for the two complexes.info:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-82991https://www.arca.fiocruz.br/bitstream/icict/56114/1/license.txt5a560609d32a3863062d77ff32785d58MD51ORIGINALDistinctmRNA_Frontiers_Molecular_2022ok.pdfDistinctmRNA_Frontiers_Molecular_2022ok.pdfapplication/pdf2713157https://www.arca.fiocruz.br/bitstream/icict/56114/2/DistinctmRNA_Frontiers_Molecular_2022ok.pdf2772de981d5fc07d01c8ae711a25c85dMD52icict/561142022-12-21 12:45:04.778oai:www.arca.fiocruz.br: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ório InstitucionalPUBhttps://www.arca.fiocruz.br/oai/requestrepositorio.arca@fiocruz.bropendoar:21352022-12-21T15:45:04Repositório Institucional da FIOCRUZ (ARCA) - 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dc.title.en_US.fl_str_mv |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
title |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
spellingShingle |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei Bezerra, Maria J. R. EIF4E EIF4G mRNA Protein Biosynthesis Peptide Chain Initiation, Translational Eukaryotic Initiation Factor-4E Eukaryotic Initiation Factor-4G Biosíntesis de Proteínas Iniciación de la Cadena Peptídica Traduccional Factor 4E Eucariótico de Iniciación Factor 4G Eucariótico de Iniciación Biosynthèse des protéines Initiation de la traduction Facteur-4E d'initiation eucaryote Facteur-4G d'initiation eucaryote Biossíntese de Proteínas Iniciação Traducional da Cadeia Peptídica Fator de Iniciação 4E em Eucariotos Fator de Iniciação 4G em Eucariotos Trypanosoma |
title_short |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
title_full |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
title_fullStr |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
title_full_unstemmed |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
title_sort |
Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei |
author |
Bezerra, Maria J. R. |
author_facet |
Bezerra, Maria J. R. Moura, Danielle M. N. Freire, Eden R. Holetz, Fabíola Barbieri Reis, Christian R. S. Monteiro, Tallyta T. S. Pinto, Adriana R. S. Pinto Zhang, Ning Rezende, Antonio M. Pereira-Neves, Antonio Figueiredo, Regina C. B. Q. Clayton, Christine Field, Mark C. Carrington, Mark Melo Neto, Osvaldo P. de |
author_role |
author |
author2 |
Moura, Danielle M. N. Freire, Eden R. Holetz, Fabíola Barbieri Reis, Christian R. S. Monteiro, Tallyta T. S. Pinto, Adriana R. S. Pinto Zhang, Ning Rezende, Antonio M. Pereira-Neves, Antonio Figueiredo, Regina C. B. Q. Clayton, Christine Field, Mark C. Carrington, Mark Melo Neto, Osvaldo P. de |
author2_role |
author author author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Bezerra, Maria J. R. Moura, Danielle M. N. Freire, Eden R. Holetz, Fabíola Barbieri Reis, Christian R. S. Monteiro, Tallyta T. S. Pinto, Adriana R. S. Pinto Zhang, Ning Rezende, Antonio M. Pereira-Neves, Antonio Figueiredo, Regina C. B. Q. Clayton, Christine Field, Mark C. Carrington, Mark Melo Neto, Osvaldo P. de |
dc.subject.other.en_US.fl_str_mv |
EIF4E EIF4G mRNA |
topic |
EIF4E EIF4G mRNA Protein Biosynthesis Peptide Chain Initiation, Translational Eukaryotic Initiation Factor-4E Eukaryotic Initiation Factor-4G Biosíntesis de Proteínas Iniciación de la Cadena Peptídica Traduccional Factor 4E Eucariótico de Iniciación Factor 4G Eucariótico de Iniciación Biosynthèse des protéines Initiation de la traduction Facteur-4E d'initiation eucaryote Facteur-4G d'initiation eucaryote Biossíntese de Proteínas Iniciação Traducional da Cadeia Peptídica Fator de Iniciação 4E em Eucariotos Fator de Iniciação 4G em Eucariotos Trypanosoma |
dc.subject.en.en_US.fl_str_mv |
Protein Biosynthesis Peptide Chain Initiation, Translational Eukaryotic Initiation Factor-4E Eukaryotic Initiation Factor-4G |
dc.subject.es.en_US.fl_str_mv |
Biosíntesis de Proteínas Iniciación de la Cadena Peptídica Traduccional Factor 4E Eucariótico de Iniciación Factor 4G Eucariótico de Iniciación |
dc.subject.fr.en_US.fl_str_mv |
Biosynthèse des protéines Initiation de la traduction Facteur-4E d'initiation eucaryote Facteur-4G d'initiation eucaryote |
dc.subject.decs.en_US.fl_str_mv |
Biossíntese de Proteínas Iniciação Traducional da Cadeia Peptídica Fator de Iniciação 4E em Eucariotos Fator de Iniciação 4G em Eucariotos Trypanosoma |
description |
Fundação Oswaldo Cruz. Instituto Aggeu Magalhães. Recife, PE, Brasil. / Universidade Federal de Pernambuco. Departamento de Genética. Recife, PE, Brasil. |
publishDate |
2022 |
dc.date.accessioned.fl_str_mv |
2022-12-21T15:45:04Z |
dc.date.available.fl_str_mv |
2022-12-21T15:45:04Z |
dc.date.issued.fl_str_mv |
2022 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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publishedVersion |
dc.identifier.citation.fl_str_mv |
BEZERRA, Maria J. R. et al. Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei. Front. Mol. Biosci, v. 9, n. 971811, p. 1–22, 2022. |
dc.identifier.uri.fl_str_mv |
https://www.arca.fiocruz.br/handle/icict/56114 |
dc.identifier.issn.en_US.fl_str_mv |
2296-889X |
identifier_str_mv |
BEZERRA, Maria J. R. et al. Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes from Trypanosoma brucei. Front. Mol. Biosci, v. 9, n. 971811, p. 1–22, 2022. 2296-889X |
url |
https://www.arca.fiocruz.br/handle/icict/56114 |
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por |
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por |
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info:eu-repo/semantics/openAccess |
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Frontiers Media |
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Frontiers Media |
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