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