Predicting the pathway involved in post-translational modification of Elongation factor P in a subset of bacterial species |
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Authors: | Marc Bailly Valérie de Crécy-Lagard |
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Institution: | (1) Department of Microbiology and Cell Science, University of Florida, Gainesville, FL, USA |
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Abstract: | Background The bacterial elongation factor P (EF-P) is strictly conserved in bacteria and essential for protein synthesis. It is homologous
to the eukaryotic translation initiation factor 5A (eIF5A). A highly conserved eIF5A lysine is modified into an unusual amino
acid derived from spermidine, hypusine. Hypusine is absolutely required for eIF5A's role in translation in Saccharomyces cerevisiae. The homologous lysine of EF-P is also modified to a spermidine derivative in Escherichia coli. However, the biosynthesis pathway of this modification in the bacterial EF-P is yet to be elucidated. |
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