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Behr, S.* ; Kristoficova, I.* ; Witting, M. ; Breland, E.J.* ; Eberly, A.R.* ; Sachs, C.* ; Schmitt-Kopplin, P. ; Hadjifrangiskou, M.* ; Jung, K.*

Identification of a high-affinity pyruvate receptor in escherichia coli.

Sci. Rep. 7:1388 (2017)
Publ. Version/Full Text Research data DOI PMC
Open Access Gold
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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.
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Publication type Article: Journal article
Document type Scientific Article
Language english
Publication Year 2017
HGF-reported in Year 2017
ISSN (print) / ISBN 2045-2322
e-ISSN 2045-2322
Journal Scientific Reports
Quellenangaben Volume: 7, Issue: 1, Pages: , Article Number: 1388 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Research Unit BioGeoChemistry and Analytics (BGC)
POF-Topic(s) 30202 - Environmental Health
Research field(s) Environmental Sciences
PSP Element(s) G-504800-001
PubMed ID 28469239
DOI 10.1038/s41598-017-01410-2
WOS ID WOS:000400490600013
Scopus ID 85018753433
Erfassungsdatum 2017-07-05
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