YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars

Abstract In Bacillus subtilis, Listeria monocytogenes and in two Mycobacteria, it was previously shown that yvcK is a gene required for normal cell shape, for optimal carbon source utilization and for virulence of pathogenic bacteria. Here we report that the B. subtilis protein YvcK binds to Uridine...

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Autores principales:	Elodie Foulquier, Anne Galinier
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6c3be92a1fba4dd8b3c596910dc463e6
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spelling	oai:doaj.org-article:6c3be92a1fba4dd8b3c596910dc463e62021-12-02T16:06:30ZYvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars10.1038/s41598-017-04064-22045-2322https://doaj.org/article/6c3be92a1fba4dd8b3c596910dc463e62017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04064-2https://doaj.org/toc/2045-2322Abstract In Bacillus subtilis, Listeria monocytogenes and in two Mycobacteria, it was previously shown that yvcK is a gene required for normal cell shape, for optimal carbon source utilization and for virulence of pathogenic bacteria. Here we report that the B. subtilis protein YvcK binds to Uridine diphosphate-sugars like Uridine diphosphate-Glucose (UDP-Glc) and Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) in vitro. Using the crystal structure of Bacillus halodurans YvcK, we identified residues involved in this interaction. We tested the effect of point mutations affecting the ability of YvcK to bind UDP-sugars on B. subtilis physiology and on cell size. Indeed, it was shown that UDP-Glc serves as a metabolic signal to regulate B. subtilis cell size. Interestingly, we observed that, whereas a yvcK deletion results in the formation of unusually large cells, inactivation of YvcK UDP-sugar binding site does not affect cell length. However, these point mutations result in an increased sensitivity to bacitracin, an antibiotic which targets peptidoglycan synthesis. We thus propose that UDP-GlcNAc, a precursor of peptidoglycan, could be a good physiological ligand candidate of YvcK.Elodie FoulquierAnne GalinierNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Elodie Foulquier Anne Galinier YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
description	Abstract In Bacillus subtilis, Listeria monocytogenes and in two Mycobacteria, it was previously shown that yvcK is a gene required for normal cell shape, for optimal carbon source utilization and for virulence of pathogenic bacteria. Here we report that the B. subtilis protein YvcK binds to Uridine diphosphate-sugars like Uridine diphosphate-Glucose (UDP-Glc) and Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) in vitro. Using the crystal structure of Bacillus halodurans YvcK, we identified residues involved in this interaction. We tested the effect of point mutations affecting the ability of YvcK to bind UDP-sugars on B. subtilis physiology and on cell size. Indeed, it was shown that UDP-Glc serves as a metabolic signal to regulate B. subtilis cell size. Interestingly, we observed that, whereas a yvcK deletion results in the formation of unusually large cells, inactivation of YvcK UDP-sugar binding site does not affect cell length. However, these point mutations result in an increased sensitivity to bacitracin, an antibiotic which targets peptidoglycan synthesis. We thus propose that UDP-GlcNAc, a precursor of peptidoglycan, could be a good physiological ligand candidate of YvcK.
format	article
author	Elodie Foulquier Anne Galinier
author_facet	Elodie Foulquier Anne Galinier
author_sort	Elodie Foulquier
title	YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
title_short	YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
title_full	YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
title_fullStr	YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
title_full_unstemmed	YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
title_sort	yvck, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6c3be92a1fba4dd8b3c596910dc463e6
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YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars

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