PMID:23239623
| Citation |
Ude, S, Lassak, J, Starosta, AL, Kraxenberger, T, Wilson, DN and Jung, K (2013) Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. Science 339:82-5 |
|---|---|
| Abstract |
Translation elongation factor P (EF-P) is critical for virulence in bacteria. EF-P is present in all bacteria and orthologous to archaeal and eukaryotic initiation factor 5A, yet the biological function has so far remained enigmatic. Here, we demonstrate that EF-P is an elongation factor that enhances translation of polyproline-containing proteins: In the absence of EF-P, ribosomes stall at polyproline stretches, whereas the presence of EF-P alleviates the translational stalling. Moreover, we demonstrate the physiological relevance of EF-P to fine-tune the expression of the polyproline-containing pH receptor CadC to levels necessary for an appropriate stress response. Bacterial, archaeal, and eukaryotic cells have hundreds to thousands of polyproline-containing proteins of diverse function, suggesting that EF-P and a/eIF-5A are critical for copy-number adjustment of multiple pathways across all kingdoms of life. |
| Links |
PubMed Online version:10.1126/science.1228985 |
| Keywords |
Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/genetics; Hydrogen-Ion Concentration; Peptide Chain Elongation, Translational; Peptide Elongation Factors/genetics; Peptide Elongation Factors/metabolism; Peptides/genetics; Peptides/metabolism; Ribosomes/metabolism; Stress, Physiological; Trans-Activators/biosynthesis; Trans-Activators/genetics |
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