OmpA, a Common Virulence Factor, Is Under RNA Thermometer Control in Yersinia pseudotuberculosis.
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This article found evidence for temperature-modulated RNA structure in the 5'-untranslated region (5'-UTR) of the Yersinia pseudotuberculosis ompA transcript suggesting that opening of the structure at host-body temperature might relieve translational repression.Abstract:
The outer membrane protein OmpA is a virulence factor in many mammalian pathogens. In previous global RNA structure probing studies, we found evidence for a temperature-modulated RNA structure in the 5'-untranslated region (5'-UTR) of the Yersinia pseudotuberculosis ompA transcript suggesting that opening of the structure at host-body temperature might relieve translational repression. Here, we support this hypothesis by quantitative reverse transcription PCR, translational reporter gene fusions, enzymatic RNA structure probing, and toeprinting assays. While ompA transcript levels decreased at 37°C compared to 25°C, translation of the transcript increased with increasing temperature. Biochemical experiments show that this is due to melting of the RNA structure, which permits ribosome binding to the 5'-UTR. A point mutation that locks the RNA structure in a closed conformation prevents translation by impairing ribosome access. Our findings add another common virulence factor to the growing list of pathogen-associated genes that are under RNA thermometer control.read more
Citations
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References
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A Novel Interaction of Outer Membrane Protein A with C4b Binding Protein Mediates Serum Resistance of Escherichia coli K1.
TL;DR: It is reported that outer membrane protein A of Escherichia coli contributes to serum resistance by binding to C4b binding protein (C4bp), a complement fluid phase regulator, and it is demonstrated that the N terminus of OmpA interacts with C4bp.
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TL;DR: An NMR‐based computational model for complexation between the PGN and OmpA emerged, and this model is validated by determining the crystal structure in complex with a synthetic PGN fragment.
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FourU: a novel type of RNA thermometer in Salmonella
TL;DR: This work has identified a new type of RNA thermometer in the 5′‐UTR of the Salmonella agsA gene, which codes for a small heat shock protein, and proposes to name ‘fourU’ thermometers, which are based on a stretch of four uridines that pair with the SD sequence.
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Concerted Actions of a Thermo-labile Regulator and a Unique Intergenic RNA Thermosensor Control Yersinia Virulence
Katja Böhme,Rebekka Steinmann,Jens Kortmann,Stephanie Seekircher,Ann Kathrin Heroven,Evelin Berger,Fabio Pisano,Tanja Thiermann,Hans Wolf-Watz,Franz Narberhaus,Petra Dersch +10 more
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TolB protein of Escherichia coli K‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA
TL;DR: It is proposed that TolB and Pal are part of a multiprotein complex that links the peptidoglycan to the outer membrane and might form transenvelope complexes that bring the two membranes into close proximity and help some outer membrane components to reach their final destination.