Author | Reolon, Lidia Watanabe | |
Author | Vichier-Guerre, Sophie | |
Author | Matos, Bruno Moisés de | |
Author | Dugué, Laurence | |
Author | Assunção, Tatiana Reichert da Silva | |
Author | Zanchin, Nilson Ivo Tonin | |
Author | Pochet, Sylvie | |
Author | Guimarães, Beatriz Gomes | |
Access date | 2019-09-30T19:11:33Z | |
Available date | 2019-09-30T19:11:33Z | |
Document date | 2019 | |
Citation | REOLON, Lídia Watanabe et al. Crystal structure of the Trypanosoma cruzi EIF4E5 translation factor homologue in complex with mRNA cap-4. Nucleic Acids Research, v. 47, n. 11, p. 5973-5987, 2019. | pt_BR |
ISSN | 0305-1048 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/36012 | |
Language | por | pt_BR |
Publisher | Oxford University Press | pt_BR |
Rights | open access | pt_BR |
Subject in Portuguese | Trypanosomatina | pt_BR |
Title | Crystal structure of the Trypanosoma cruzi EIF4E5 translation factor homologue in complex with mRNA cap-4 | pt_BR |
Type | Article | pt_BR |
DOI | 10.1093/nar/gkz339 | |
Abstract | Association of the initiation factor eIF4E with the mRNA cap structure is a key step for translation. Trypanosomatids present six eIF4E homologues, showing a low conservation and also differing significantly from the IF4Es of multicellular eukaryotes. On the mRNA side, while in most eukaryotes the mRNA contains cap-0 (7-methyl-GTP), the trypanosomatid mRNA features a cap-4, which is formed by a cap-0, followed by the AACU sequence containing 2'-O-ribose methylations and base methylations on nucleotides 1 and 4. The studies on eIF4E-cap-4 interaction have been hindered by the difficulty to synthesize this rather elaborated cap-4 sequence. To overcome this problem, we applied a liquid-phase oligonucleotide synthesis strategy and describe for the first time the crystal structure of a trypanosomatid eIF4E (T. cruzi EIF4E5) in complex with cap-4. The TcEIF4E5-cap-4 structure allowed a detailed description of the binding mechanism, revealing the interaction mode for the AACU sequence, with the bases packed in a parallel stacking conformation and involved, together with the methyl groups, in hydrophobic contacts with the protein. This binding mechanism evidences a distinct cap interaction mode in comparison with previously described eIF4E structures and may account for the difference of TcEIF4E5-cap-4 dissociation constant in comparison with other eIF4E homologues. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil / Universidade Federal do Paraná. Programa de Pós-Graduação em Ciências - Bioquímica. Curitiba, PR, Brasil. | pt_BR |
Affilliation | Institut Pasteur. Unité de Chimie et Biocatalyse. Paris, France. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil / Universidade Federal do Paraná. Programa de Pós-Graduação em Ciências - Bioquímica. Curitiba, PR, Brasil. | pt_BR |
Affilliation | Institut Pasteur. Unité de Chimie et Biocatalyse. Paris, France. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil. | pt_BR |
Affilliation | Institut Pasteur. Unité de Chimie et Biocatalyse. Paris, France. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil / Universidade Federal do Paraná. Programa de Pós-Graduação em Ciências - Bioquímica. Curitiba, PR, Brasil. | pt_BR |
Subject | Eukaryotic Initiation Factor-4E | pt_BR |
Subject | RNA Cap-Binding Proteins | pt_BR |
Subject in Spanish | Factor 4E Eucariótico de Iniciación | pt_BR |
Subject in Spanish | Proteínas de Unión a Caperuzas de ARN | pt_BR |
DeCS | Fator de Iniciação 4E em Eucariotos | pt_BR |
DeCS | Proteínas de Ligação ao Cap de RNA | pt_BR |
e-ISSN | 1362-4962 | |