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Updated: Jun 5, 2025

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
Published on: May 1, 2020
Trypanosoma cruzi eIF4E3- and eIF4E4-containing complexes bind different mRNAs and may sequester inactive mRNAs
Bernardo Papini Gabiatti1,2, Eden Ribeiro Freire1, Jimena Ferreira da Costa1
1Carlos Chagas Institute, Oswaldo Cruz Foundation, FIOCRUZ, R. Prof. Algacyr Munhoz Mader 3775, 81350-010, Curitiba-PR, Brazil.
Abstract:
Many eIF4F and poly(A)-binding protein (PABP) paralogues are found in trypanosomes: six eIF4E, five eIF4G, one eIF4A and two PABPs. They are expressed simultaneously and assemble into different complexes, contrasting the situation in metazoans that use distinct complexes in different cell types/developmental stages. Each eIF4F complex has its own proteins, messenger RNAs (mRNAs) and, consequently, a distinct function. We set out to study the function and regulation of the two eIF4F complexes of the parasite Trypanosoma cruzi and identified the associated proteins and mRNAs of eIF4E3 and eIF4E4 in cells in exponential growth and in nutritional stress, an inducer of differentiation to an infective stage. Upon stress, eIF4G and PABP remain associated with the eIF4E, but the associations with other 43S pre-initiation factors decrease, indicating ribosome attachment is impaired. Most eIF4E3-associated mRNAs encode for proteins involved in anabolic metabolism, while eIF4E4 associate with mRNAs encoding ribosomal proteins as in Trypanosoma brucei. Interestingly, for both eIF4E3/4, more mRNAs were associated in stressed cells than in non-stressed cells, even though these have lower translational efficiencies in stress. In summary, trypanosomes have two co-existing eIF4F complexes associating to different mRNAs, but not stress/differentiation-associated mRNAs. Under stress, both complexes exit translation but remain bound to their mRNA targets.
Insights
Trypanosomes utilize two distinct eIF4F complexes, each binding specific messenger RNAs (mRNAs). Under stress, these complexes halt translation but maintain mRNA binding, impacting parasite differentiation.
Area of Science:
- Molecular Biology
- Parasitology
- Gene Regulation
Background:
- Trypanosomes possess multiple paralogues of translation initiation factors like eIF4F and poly(A)-binding proteins (PABPs), unlike metazoans.
- These factors assemble into distinct complexes, each associated with specific messenger RNAs (mRNAs) and performing unique functions.
Purpose of the Study:
- To investigate the function and regulation of the two eIF4F complexes (eIF4E3 and eIF4E4) in the parasite *Trypanosoma cruzi*.
- To identify associated proteins and mRNAs under conditions of exponential growth and nutritional stress, which induces differentiation.
Main Methods:
- Analysis of protein and mRNA associations with eIF4E3 and eIF4E4 complexes.
- Comparison of complex composition and mRNA binding under growth and stress conditions.
Main Results:
- Two distinct eIF4F complexes (eIF4E3 and eIF4E4) were identified, each binding to different sets of mRNAs.
- Under nutritional stress, eIF4G and PABP remain associated with eIF4E, but ribosome attachment is reduced, indicating impaired translation initiation.
- eIF4E3-associated mRNAs primarily encode anabolic metabolism proteins, while eIF4E4 associates with ribosomal protein mRNAs.
- Despite lower translational efficiency under stress, both complexes bind to a greater number of mRNAs compared to non-stressed conditions.
Conclusions:
- *Trypanosoma cruzi* employs two co-existing eIF4F complexes that bind distinct mRNA populations.
- During stress-induced differentiation, these complexes exit translation but remain associated with their target mRNAs, suggesting a regulatory role beyond active translation.
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