ArticleRNA (New York, N.Y.)2004
Cap-binding activity of an eIF4E homolog from Leishmania.
Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 47 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
- CMTr cap-adjacent 2'-O-ribose mRNA methyltransferases are required for reward learning and mRNA localization to synapses.Nature communications · 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
- Taking a re-look at cap-binding signatures of the mRNA cap-binding protein eIF4E orthologues in trypanosomatids.Molecular and cellular biochemistry · 2021Review
- Article
- Regulation of gene expression in trypanosomatids: living with polycistronic transcription.Open biology · 2019Article
- The suppressive cap-binding complex factor 4EIP is required for normal differentiation.Nucleic acids research · 2018Article
- Analysis of the Antigenic and Prophylactic Properties of theFrontiers in cellular and infection microbiology · 2018Article
- The Role of Cytoplasmic mRNA Cap-Binding Protein Complexes in Trypanosoma brucei and Other Trypanosomatids.Pathogens (Basel, Switzerland) · 2017Review
- The eIF3 complex of Leishmania-subunit composition and mode of recruitment to different cap-binding complexes.Nucleic acids research · 2015Article
- Distinct features of cap binding by eIF4E1b proteins.Journal of molecular biology · 2015Article
- Differential Subcellular Localization of Leishmania Alba-Domain Proteins throughout the Parasite Development.PloS one · 2015Article
- eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei.RNA (New York, N.Y.) · 2014Article
- Comparative ribosome profiling reveals extensive translational complexity in different Trypanosoma brucei life cycle stages.Nucleic acids research · 2014Article
- RNA Granules Living a Post-transcriptional Life: the Trypanosomes' Case.Current chemical biology · 2011Article
- The four trypanosomatid eIF4E homologues fall into two separate groups, with distinct features in primary sequence and biological properties.Molecular and biochemical parasitology · 2011Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All eukaryotic mRNAs possess a 5'-cap (m(7)GpppN) that is recognized by a family of cap-binding proteins. These participate in various processes, such as RNA transport and stabilization, as well as in assembly of the translation initiation complex. The 5'-cap of trypanosomatids is complex; in addition to 7-methyl guanosine, it includes unique modifications on the first four transcribed nucleotides, and is thus denoted cap-4. Here we analyze a cap-binding protein of Leishmania, in an attempt to understand the structural features that promote its binding to this unusual cap. LeishIF4E-1, a homolog of eIF4E, contains the conserved cap-binding pocket, similar to its mouse counterpart. The mouse eIF4E has a higher K(as) for all cap analogs tested, as compared with LeishIF4E-1. However, whereas the mouse eIF4E shows a fivefold higher affinity for m(7)GTP than for a chemically synthesized cap-4 structure, LeishIF4E-1 shows similar affinities for both ligands. A sequence alignment shows that LeishIF4E-1 lacks the region that parallels the C terminus in the murine eIF4E. Truncation of this region in the mouse protein reduces the difference that is observed between its binding to m(7)GTP and cap-4, prior to this deletion. We hypothesize that variations in the structure of LeishIF4E-1, possibly also the absence of a region that is homologous to the C terminus of the mouse protein, promote its ability to interact with the cap-4 structure. LeishIF4E-1 is distributed in the cytoplasm, but its function is not clear yet, because it cannot substitute the mammalian eIF4E in a rabbit reticulocyte in vitro translation system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.