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Ethanolamine phosphoglycerol (EPG) is a protein modification attached exclusively to eukaryotic elongation factor 1A (eEF1A). In mammals and plants, EPG is linked to conserved glutamate residues located in eEF1A domains II and III, whereas in the unicellular eukaryote  Trypanosoma brucei , only domain III is modified by a single EPG. A biosynthetic precursor of EPG and structural requirements for EPG attachment to  T. brucei  eEF1A have been reported, but nothing is known about the EPG modifying enzyme(s). By expressing human eEF1A in  T. brucei , we now show that EPG attachment to eEF1A is evolutionarily conserved between  T. brucei  and  Homo sapiens . In contrast,  S. cerevisiae  eEF1A, which has been shown to lack EPG is not modified in  T. brucei.  Furthermore, we show that eEF1A cannot functionally complement across species when using  T. brucei  and  S. cerevisiae  as model organisms. However, functional complementation in yeast can be obtained using eEF1A chimera containing domains II or III from other species. In contrast, yeast domain I is strictly required for functional complementation in  S. cerevisiae .

Eukaryotic Translation Elongation Factor 1A (eEF1A) Domain I from S. cerevisiae Is Required but Not Sufficient for Inter-Species Complementation