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Eukaryotic translation initiation factor 5A (eIF5A) is a highly conserved and essential protein in eukaryotes, playing a critical role in mRNA translation, particularly during the elongation phase. The unique feature of eIF5A is its post-translational modification at lysine residue 50 (K50), where the polyamine spermidine is enzymatically added to form hypusine. The K50R mutant is a specific variant of eIF5A in which lysine at position 50 is replaced by arginine. This substitution prevents the formation of hypusine, resulting in an inactive or non-functional form of eIF5A with respect to its canonical roles. This mutant is primarily used as a research tool to study the effects of hypusination deficiency.
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