ArticleEukaryotic cell2006
Binding specificities and potential roles of isoforms of eukaryotic initiation factor 4E in Leishmania.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 79 citations in OpenAlex.
- Five-layer systems analysis ofeLife · 2026Article
- Trypanosomatid DRBD9s are likely to be eIF4B orthologues.Journal of biosciences · 2025Article
- LeishIF3d is a non-canonical cap-binding protein inFrontiers in molecular biosciences · 2023Article
- Experimental evolution links post-transcriptional regulation to Leishmania fitness gain.PLoS pathogens · 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
- TheGenes · 2021Article
- Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021Article
- Article
- A newly identified Leishmania IF4E-interacting protein, Leish4E-IP2, modulates the activity of cap-binding protein paralogs.Nucleic acids research · 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
- Regulation of Germ Cell mRNPs by eIF4E:4EIP Complexes: Multiple Mechanisms, One Goal.Frontiers in cell and developmental biology · 2020Review
- Article
- Deletion of a Single LeishIF4E-3 Allele by the CRISPR-Cas9 System Alters Cell Morphology and Infectivity ofmSphere · 2019Article
- 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
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Authors and funding
8 authors at 3 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The 5' cap structure of trypanosomatid mRNAs, denoted cap 4, is a complex structure that contains unusual modifications on the first four nucleotides. We examined the four eukaryotic initiation factor 4E (eIF4E) homologues found in the Leishmania genome database. These proteins, denoted LeishIF4E-1 to LeishIF4E-4, are located in the cytoplasm. They show only a limited degree of sequence homology with known eIF4E isoforms and among themselves. However, computerized structure prediction suggests that the cap-binding pocket is conserved in each of the homologues, as confirmed by binding assays to m(7)GTP, cap 4, and its intermediates. LeishIF4E-1 and LeishIF4E-4 each bind m(7)GTP and cap 4 comparably well, and only these two proteins could interact with the mammalian eIF4E binding protein 4EBP1, though with different efficiencies. 4EBP1 is a translation repressor that competes with eIF4G for the same residues on eIF4E; thus, LeishIF4E-1 and LeishIF4E-4 are reasonable candidates for serving as translation factors. LeishIF4E-1 is more abundant in amastigotes and also contains a typical 3' untranslated region element that is found in amastigote-specific genes. LeishIF4E-2 bound mainly to cap 4 and comigrated with polysomal fractions on sucrose gradients. Since the consensus eIF4E is usually found in 48S complexes, LeishIF4E-2 could possibly be associated with the stabilization of trypanosomatid polysomes. LeishIF4E-3 bound mainly m(7)GTP, excluding its involvement in the translation of cap 4-protected mRNAs. It comigrates with 80S complexes which are resistant to micrococcal nuclease, but its function is yet unknown. None of the isoforms can functionally complement the Saccharomyces cerevisiae eIF4E, indicating that despite their structural conservation, they are considerably diverged.
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