ArticleEukaryotic cell2014
Trypanosoma brucei translation initiation factor homolog EIF4E6 forms a tripartite cytosolic complex with EIF4G5 and a capping enzyme homolog.
Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 45 citations in OpenAlex.
- Trypanosoma cruzi eIF4E3- and eIF4E4-containing complexes bind different mRNAs and may sequester inactive mRNAs during nutritional stress.Nucleic acids research · 2025Article
- Trypanosomatid DRBD9s are likely to be eIF4B orthologues.Journal of biosciences · 2025Article
- Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits.Scientific reports · 2024Article
- Analysis of domain organization and functional signatures of trypanosomatid keIF4Gs.Molecular and cellular biochemistry · 2022Article
- Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes fromFrontiers in molecular biosciences · 2022Article
- The translation initiation factor EIF4E5 from Leishmania: crystal structure and interacting partners.RNA biology · 2021Article
- Characterization of an Atypical eIF4E Ortholog inInternational journal of molecular sciences · 2021Article
- LeishIF4E-5 Is a Promastigote-Specific Cap-Binding Protein inInternational journal of molecular sciences · 2021Article
- Distinct features of the Leishmania cap-binding protein LeishIF4E2 revealed by CRISPR-Cas9 mediated hemizygous deletion.PLoS neglected tropical diseases · 2021Article
- Taking a re-look at cap-binding signatures of the mRNA cap-binding protein eIF4E orthologues in trypanosomatids.Molecular and cellular biochemistry · 2021Review
- Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021Article
- The RNA-associated proteins MKT1 and MKT1L form alternative PBP1-containing complexes inThe Journal of biological chemistry · 2020Article
- Regulation of Translation in the Protozoan ParasiteInternational journal of molecular sciences · 2020Review
- eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020Review
- Crystal structure of the MIF4G domain of the Trypanosoma cruzi translation initiation factor EIF4G5.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Article
- Regulation of gene expression in trypanosomatids: living with polycistronic transcription.Open biology · 2019Article
- Crystal structure of the Trypanosoma cruzi EIF4E5 translation factor homologue in complex with mRNA cap-4.Nucleic acids research · 2019Article
- Nutritional stress targets LeishIF4E-3 to storage granules that contain RNA and ribosome components in Leishmania.PLoS neglected tropical diseases · 2019Article
- A recap of RNA recapping.Wiley interdisciplinary reviews. RNA · 2019Review
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Authors and funding
14 authors at 3 institutions in 3 countries.
Funding
Abstract
Trypanosomes lack the transcriptional control characteristic of the majority of eukaryotes that is mediated by gene-specific promoters in a one-gene-one-promoter arrangement. Rather, their genomes are transcribed in large polycistrons with no obvious functional linkage. Posttranscriptional regulation of gene expression must thus play a larger role in these organisms. The eIF4E homolog TbEIF4E6 binds mRNA cap analogs in vitro and is part of a complex in vivo that may fulfill such a role. Knockdown of TbEIF4E6 tagged with protein A-tobacco etch virus protease cleavage site-protein C to approximately 15% of the normal expression level resulted in viable cells that displayed a set of phenotypes linked to detachment of the flagellum from the length of the cell body, if not outright flagellum loss. While these cells appeared and behaved as normal under stationary liquid culture conditions, standard centrifugation resulted in a marked increase in flagellar detachment. Furthermore, the ability of TbEIF4E6-depleted cells to engage in social motility was reduced. The TbEIF4E6 protein forms a cytosolic complex containing a triad of proteins, including the eIF4G homolog TbEIF4G5 and a hypothetical protein of 70.3 kDa, referred to as TbG5-IP. The TbG5-IP analysis revealed two domains with predicted secondary structures conserved in mRNA capping enzymes: nucleoside triphosphate hydrolase and guanylyltransferase. These complex members have the potential for RNA interaction, either via the 5' cap structure for TbEIF4E6 and TbG5-IP or through RNA-binding domains in TbEIF4G5. The associated proteins provide a signpost for future studies to determine how this complex affects capped RNA molecules.
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