Identification of a High-Affinity Pyruvate Receptor in Escherichia coli.
Authors Behr S, Kristoficova I, Witting M, Breland EJ, Eberly AR, Sachs C,
Schmitt-Kopplin P, Hadjifrangiskou M, Jung K
Submitted By Submitted Externally on 5/23/2017
Status Published
Journal Scientific reports
Year 2017
Date Published 5/1/2017
Volume : Pages 7 : 1388
PubMed Reference 28469239
Abstract Two-component systems are crucial for signal perception and modulation of
bacterial behavior. Nevertheless, to date, very few ligands have been identified
that directly interact with histidine kinases. The histidine kinase/response
regulator system YehU/YehT of Escherichia coli is part of a nutrient-sensing
network. Here we demonstrate that this system senses the onset of nutrient
limitation in amino acid rich media and responds to extracellular pyruvate.
Binding of radiolabeled pyruvate was found for full-length YehU in
right-side-out membrane vesicles as well as for a truncated, membrane-integrated
variant, confirming that YehU is a high-affinity receptor for extracellular
pyruvate. Therefore we propose to rename YehU/YehT as BtsS/BtsR, after
"Brenztraubensäure", the name given to pyruvic acid when it was first
synthesized. The function of BtsS/BtsR was also assessed in a clinically
relevant uropathogenic E. coli strain. Quantitative transcriptional analysis
revealed BtsS/BtsR importance during acute and chronic urinary-tract infections.