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Investigation of the conserved glutamate immediately following the DEAD box in eukaryotic translation initiation factor 4AI

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The DExD-box family (DEAD-box) of proteins was surveyed for eukaryotic translation initiation factor 4A-specific sequences surrounding the DEAD box. An eIF4A-unique glutamate residue (E186 in eIF4AI) was identified immediately following the D-E-A-D sequence in eIF4AI, II, and III that was found to be conserved from yeast to Man. Mutation to a selection of alternative amino acids was performed within recombinant eIF4AI expressed in Escherichia coli and mutant proteins were surveyed for RNA-dependent ATPase activity. The mutants were also investigated for changes in activity in the presence of the two eIF4AI-binding domains of eIF4GI as well as for co-purification ability to these two domains. The E186 residue was found to be of significance for RNA-dependent ATPase activity for eIF4AI alone and in the presence of eIF4AI-binding domains of eIF4GI through point-mutation analysis. Furthermore, binding interactions between eIF4AI and eIF4GI domains were also significantly influenced by mutation of E186, as observed through co-purification assays. Thus, this residue appears to be of functional significance for eIF4A.
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Keywords: DEAD-box family; eukaryotic translation initiation factor 4A; facteur d’initiation de la traduction; facteur d’initiation de la traduction eucaryote 4A; famille à boîte DEAD; helicase; hélicase, superfamille 2; superfamily 2; translation initiation factor

Document Type: Research Article

Publication date: January 1, 2014

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