Reference - Detail
RRC ID | 35589 |
---|---|
Author | Ude S, Lassak J, Starosta AL, Kraxenberger T, Wilson DN, Jung K. |
Title | Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. |
Journal | Science |
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. |
Volume | 339(6115) |
Pages | 82-5 |
Published | 2013-1-4 |
DOI | 10.1126/science.1228985 |
PII | science.1228985 |
PMID | 23239623 |
MeSH | 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 |
IF | 41.846 |
Times Cited | 224 |
WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY |
Resource | |
Prokaryotes E. coli | ME9062(BW25113) JW4116-KC JW4106-KC JW4094-KC |