Analysis of domain organization and functional signatures of trypanosomatid keIF4Gs.

Translation initiation is the first step in three essential processes leading to protein synthesis. It is carried out by proteins called translation initiation factors and ribosomes on the mRNA. One of the critical translation initiation factors in eukaryotes is eIF4G which is a scaffold protein that helps assemble translation initiation complexes that carry out translation initiation which ultimately leads to polypeptide synthesis. Trypanosomatids are a large family of kinetoplastids, some of which are protozoan parasites that cause diseases in humans through transmission by vectors. While the protein translation mechanisms in eukaryotes and prokaryotes are well understood, the protein translation factors and mechanisms in trypanosomatids are poorly understood necessitating further studies. Unlike other eukaryotes, trypanosomatids contain five eIF4G orthologues with diversity in length and sequences. Here, I have used bioinformatics tools to look at trypanosomatid keIF4G orthologue sequences and report that there are similarities and considerable differences in their domains/motifs organization and signature amino acid sequences that are required for different functions as compared to human eIF4G. My analysis suggests that there is likely to be considerable diversity and complexity in trypanosomatid keIF4G functions as compared to other eukaryotes.