Identification of a High-Affinity Pyruvate Receptor in Escherichia coli

Stefan Behr, Ivica Kristoficova, Michael Witting, Erin J. Breland, Allison R. Eberly, Corinna Sachs, Philippe Schmitt-Kopplin, Maria Hadjifrangiskou, Kirsten Jung

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


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 "Brenztraubensaüre", 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.

Original languageEnglish
Article number1388
JournalScientific reports
Issue number1
StatePublished - Dec 1 2017


Dive into the research topics of 'Identification of a High-Affinity Pyruvate Receptor in Escherichia coli'. Together they form a unique fingerprint.

Cite this