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2014 ; 49
(5
): 413-25
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The hypusine-containing translation factor eIF5A
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Dever TE
; Gutierrez E
; Shin BS
Crit Rev Biochem Mol Biol
2014[Sep]; 49
(5
): 413-25
PMID25029904
show ga
In addition to the small and large ribosomal subunits, aminoacyl-tRNAs, and an
mRNA, cellular protein synthesis is dependent on translation factors. The
eukaryotic translation initiation factor 5A (eIF5A) and its bacterial ortholog
elongation factor P (EF-P) were initially characterized based on their ability to
stimulate methionyl-puromycin (Met-Pmn) synthesis, a model assay for protein
synthesis; however, the function of these factors in cellular protein synthesis
has been difficult to resolve. Interestingly, a conserved lysine residue in eIF5A
is post-translationally modified to hypusine and the corresponding lysine residue
in EF-P from at least some bacteria is modified by the addition of a ?-lysine
moiety. In this review, we provide a summary of recent data that have identified
a novel role for the translation factor eIF5A and its hypusine modification in
the elongation phase of protein synthesis and more specifically in stimulating
the production of proteins containing runs of consecutive proline residues.
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