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Crystal structure of the MIF4G domain of the Trypanosoma cruzi translation initiation factor EIF4G5
Author(s) -
Camillo dos Santos Lucca Pietro,
de Matos Bruno Moisés,
de Maman Ribeiro Brenda Cecilia,
Zanchin Nilson Ivo Tonin,
Guimarães Beatriz Gomes
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19015061
Subject(s) - eif4g , eif4e , biology , initiation factor , eukaryotic translation , rna helicase a , translation (biology) , microbiology and biotechnology , rna , eif4a , eukaryotic initiation factor , rna binding protein , helicase , genetics , messenger rna , gene
Kinetoplastida, a class of early‐diverging eukaryotes that includes pathogenic Trypanosoma and Leishmania species, display key differences in their translation machinery compared with multicellular eukaryotes. One of these differences involves a larger number of genes encoding eIF4E and eIF4G homologs and the interaction pattern between the translation initiation factors. eIF4G is a scaffold protein which interacts with the mRNA cap‐binding factor eIF4E, the poly(A)‐binding protein, the RNA helicase eIF4A and the eIF3 complex. It contains the so‐called middle domain of eIF4G (MIF4G), a multipurpose adaptor involved in different protein–protein and protein–RNA complexes. Here, the crystal structure of the MIF4G domain of T. cruzi EIF4G5 is described at 2.4 Å resolution, which is the first three‐dimensional structure of a trypanosomatid MIF4G domain to be reported. Structural comparison with IF4G homologs from other eukaryotes and other MIF4G‐containing proteins reveals differences that may account for the specific interaction mechanisms of MIF4G despite its highly conserved overall fold.