Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems

Abstract Azotobacter vinelandii, a strict aerobic, nitrogen fixing bacterium in the Pseudomonadaceae family, exhibits a preferential use of acetate over glucose as a carbon source. In this study, we show that GluP (Avin04150), annotated as an H+-coupled glucose-galactose symporter, is the glucose tr...

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Autores principales:	Elva Quiroz-Rocha, Renata Moreno, Armando Hernández-Ortíz, Juan Carlos Fragoso-Jiménez, Luis Felipe Muriel-Millán, Josefina Guzmán, Guadalupe Espín, Fernando Rojo, Cinthia Núñez
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2b504a2754e644e2905d941e1b063a43
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spelling	oai:doaj.org-article:2b504a2754e644e2905d941e1b063a432021-12-02T15:05:07ZGlucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems10.1038/s41598-017-00980-52045-2322https://doaj.org/article/2b504a2754e644e2905d941e1b063a432017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00980-5https://doaj.org/toc/2045-2322Abstract Azotobacter vinelandii, a strict aerobic, nitrogen fixing bacterium in the Pseudomonadaceae family, exhibits a preferential use of acetate over glucose as a carbon source. In this study, we show that GluP (Avin04150), annotated as an H+-coupled glucose-galactose symporter, is the glucose transporter in A. vinelandii. This protein, which is widely distributed in bacteria and archaea, is uncommon in Pseudomonas species. We found that expression of gluP was under catabolite repression control thorugh the CbrA/CbrB and Crc/Hfq regulatory systems, which were functionally conserved between A. vinelandii and Pseudomonas species. While the histidine kinase CbrA was essential for glucose utilization, over-expression of the Crc protein arrested cell growth when glucose was the sole carbon source. Crc and Hfq proteins from either A. vinelandii or P. putida could form a stable complex with an RNA A-rich Hfq-binding motif present in the leader region of gluP mRNA. Moreover, in P. putida, the gluP A-rich Hfq-binding motif was functional and promoted translational inhibition of a lacZ reporter gene. The fact that gluP is not widely distributed in the Pseudomonas genus but is under control of the CbrA/CbrB and Crc/Hfq systems demonstrates the relevance of these systems in regulating metabolism in the Pseudomonadaceae family.Elva Quiroz-RochaRenata MorenoArmando Hernández-OrtízJuan Carlos Fragoso-JiménezLuis Felipe Muriel-MillánJosefina GuzmánGuadalupe EspínFernando RojoCinthia NúñezNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Elva Quiroz-Rocha Renata Moreno Armando Hernández-Ortíz Juan Carlos Fragoso-Jiménez Luis Felipe Muriel-Millán Josefina Guzmán Guadalupe Espín Fernando Rojo Cinthia Núñez Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems
description	Abstract Azotobacter vinelandii, a strict aerobic, nitrogen fixing bacterium in the Pseudomonadaceae family, exhibits a preferential use of acetate over glucose as a carbon source. In this study, we show that GluP (Avin04150), annotated as an H+-coupled glucose-galactose symporter, is the glucose transporter in A. vinelandii. This protein, which is widely distributed in bacteria and archaea, is uncommon in Pseudomonas species. We found that expression of gluP was under catabolite repression control thorugh the CbrA/CbrB and Crc/Hfq regulatory systems, which were functionally conserved between A. vinelandii and Pseudomonas species. While the histidine kinase CbrA was essential for glucose utilization, over-expression of the Crc protein arrested cell growth when glucose was the sole carbon source. Crc and Hfq proteins from either A. vinelandii or P. putida could form a stable complex with an RNA A-rich Hfq-binding motif present in the leader region of gluP mRNA. Moreover, in P. putida, the gluP A-rich Hfq-binding motif was functional and promoted translational inhibition of a lacZ reporter gene. The fact that gluP is not widely distributed in the Pseudomonas genus but is under control of the CbrA/CbrB and Crc/Hfq systems demonstrates the relevance of these systems in regulating metabolism in the Pseudomonadaceae family.
format	article
author	Elva Quiroz-Rocha Renata Moreno Armando Hernández-Ortíz Juan Carlos Fragoso-Jiménez Luis Felipe Muriel-Millán Josefina Guzmán Guadalupe Espín Fernando Rojo Cinthia Núñez
author_facet	Elva Quiroz-Rocha Renata Moreno Armando Hernández-Ortíz Juan Carlos Fragoso-Jiménez Luis Felipe Muriel-Millán Josefina Guzmán Guadalupe Espín Fernando Rojo Cinthia Núñez
author_sort	Elva Quiroz-Rocha
title	Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems
title_short	Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems
title_full	Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems
title_fullStr	Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems
title_full_unstemmed	Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems
title_sort	glucose uptake in azotobacter vinelandii occurs through a glup transporter that is under the control of the cbra/cbrb and hfq-crc systems
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/2b504a2754e644e2905d941e1b063a43
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Glucose uptake in Azotobacter vinelandii occurs through a GluP transporter that is under the control of the CbrA/CbrB and Hfq-Crc systems

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