PMID:20070887
| Citation |
Bailly, M and de Crécy-Lagard, V (2010) Predicting the pathway involved in post-translational modification of elongation factor P in a subset of bacterial species. Biol. Direct 5:3 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC2821294 Online version:10.1186/1745-6150-5-3 |
| Keywords |
Amino Acid Sequence; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genes, Bacterial/genetics; Intramolecular Transferases/chemistry; Intramolecular Transferases/genetics; Lysine-tRNA Ligase/chemistry; Lysine-tRNA Ligase/genetics; Metabolic Networks and Pathways; Models, Biological; Molecular Sequence Data; Peptide Elongation Factors/chemistry; Peptide Elongation Factors/genetics; Peptide Elongation Factors/metabolism; Phylogeny; Protein Processing, Post-Translational |
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