Identification of a High-Affinity Pyruvate Receptor in Escherichia coli

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...

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Autores principales:	Stefan Behr, Ivica Kristoficova, Michael Witting, Erin J. Breland, Allison R. Eberly, Corinna Sachs, Philippe Schmitt-Kopplin, Maria Hadjifrangiskou, Kirsten Jung
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bacae06d739a435f97840db4f099ddc3
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spelling	oai:doaj.org-article:bacae06d739a435f97840db4f099ddc32021-12-02T16:08:24ZIdentification of a High-Affinity Pyruvate Receptor in Escherichia coli10.1038/s41598-017-01410-22045-2322https://doaj.org/article/bacae06d739a435f97840db4f099ddc32017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01410-2https://doaj.org/toc/2045-2322Abstract 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.Stefan BehrIvica KristoficovaMichael WittingErin J. BrelandAllison R. EberlyCorinna SachsPhilippe Schmitt-KopplinMaria HadjifrangiskouKirsten JungNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Stefan Behr Ivica Kristoficova Michael Witting Erin J. Breland Allison R. Eberly Corinna Sachs Philippe Schmitt-Kopplin Maria Hadjifrangiskou Kirsten Jung Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
description	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.
format	article
author	Stefan Behr Ivica Kristoficova Michael Witting Erin J. Breland Allison R. Eberly Corinna Sachs Philippe Schmitt-Kopplin Maria Hadjifrangiskou Kirsten Jung
author_facet	Stefan Behr Ivica Kristoficova Michael Witting Erin J. Breland Allison R. Eberly Corinna Sachs Philippe Schmitt-Kopplin Maria Hadjifrangiskou Kirsten Jung
author_sort	Stefan Behr
title	Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
title_short	Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
title_full	Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
title_fullStr	Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
title_full_unstemmed	Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
title_sort	identification of a high-affinity pyruvate receptor in escherichia coli
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/bacae06d739a435f97840db4f099ddc3
work_keys_str_mv	AT stefanbehr identificationofahighaffinitypyruvatereceptorinescherichiacoli AT ivicakristoficova identificationofahighaffinitypyruvatereceptorinescherichiacoli AT michaelwitting identificationofahighaffinitypyruvatereceptorinescherichiacoli AT erinjbreland identificationofahighaffinitypyruvatereceptorinescherichiacoli AT allisonreberly identificationofahighaffinitypyruvatereceptorinescherichiacoli AT corinnasachs identificationofahighaffinitypyruvatereceptorinescherichiacoli AT philippeschmittkopplin identificationofahighaffinitypyruvatereceptorinescherichiacoli AT mariahadjifrangiskou identificationofahighaffinitypyruvatereceptorinescherichiacoli AT kirstenjung identificationofahighaffinitypyruvatereceptorinescherichiacoli
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Identification of a High-Affinity Pyruvate Receptor in Escherichia coli

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