The translation initiation factor EIF4E5 from Leishmania: crystal structure and interacting partners

Lima, Gustavo Barbosa de; Cavalcanti, Thaíse Yasmine Vasconcelos de Lima; Brito, Adriana Neuman Albuquerque Lins Moura de; Assis, Ludmilla Arruda de; Andrade-Vieira, Rafaela Paiva; Freire, Eden R.; Assunção, Tatiana Reichert da Silva; Reis, Christian Robson de Souza; Zanchin, Nilson Ivo Tonin; Guimarães, B.G.; Neto, Osvaldo P. de Melo

doi:10.1080/15476286.2021.1918919

RNA Biology

2021

DOI: 10.1080/15476286.2021.1918919

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The translation initiation factor EIF4E5 from Leishmania: crystal structure and interacting partners

Gustavo Barbosa de Lima

Thaíse Yasmine Vasconcelos de Lima Cavalcanti

Adriana Neuman Albuquerque Lins Moura de Brito

et al.

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2024

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Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits

Penteado,

da Silva,

Moura

et al. 2024

Sci Rep

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Recognition of the mRNA 5′ end is a critical step needed for translation initiation. This step is performed by the cap binding protein eIF4E, which joins the larger eIF4G subunit to form the eIF4F complex. Trypanosomatids have a minimum of five different eIF4F-like complexes formed through specific but not well-defined interactions between four different eIF4E and five eIF4G homologues. The EIF4E6/EIF4G5 complex has been linked with the stage-specific translation of mRNAs encoding the major Trypanosoma brucei virulence factors. Here, to better define the molecular basis for the TbEIF4E6/TbEIF4G5 interaction, we describe the identification of the peptide interacting with TbEIF4E6 in the region comprising residues 79–166 of TbEIF4G5. The TbEIF4E6-TbEIF4G5_79-116 complex reconstituted with recombinant proteins is highly stable even in the absence of cap-4. The crystal structure of the complex was subsequently solved, revealing extensive interacting surfaces. Comparative analyses highlight the conservation of the overall structural arrangement of different eIF4E/eIF4G complexes. However, highly different interacting surfaces are formed with distinct binding contacts occurring both in the canonical and noncanonical elements within eIF4G and the respective eIF4E counterpart. These specific pairs of complementary interacting surfaces are likely responsible for the selective association needed for the formation of distinct eIF4F complexes in trypanosomatids.

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Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits

Penteado,

da Silva,

Moura

et al. 2024

Sci Rep

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show abstract

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The translation initiation factor EIF4E5 from Leishmania: crystal structure and interacting partners

Cited by 1 publication

References 79 publications

Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits

Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits

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