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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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-06-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-04064-2 |
| _version_ | 1818427668111032320 |
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| author | Elodie Foulquier Anne Galinier |
| author_facet | Elodie Foulquier Anne Galinier |
| author_sort | Elodie Foulquier |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-14T14:49:23Z |
| format | Article |
| id | doaj.art-6c3be92a1fba4dd8b3c596910dc463e6 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T14:49:23Z |
| publishDate | 2017-06-01 |
| publisher | Nature Portfolio |
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| series | Scientific Reports |
| spelling | doaj.art-6c3be92a1fba4dd8b3c596910dc463e62022-12-21T22:57:11ZengNature PortfolioScientific Reports2045-23222017-06-017111110.1038/s41598-017-04064-2YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugarsElodie Foulquier0Anne Galinier1Laboratoire de Chimie Bactérienne, CNRS - Aix Marseille UnivLaboratoire de Chimie Bactérienne, CNRS - Aix Marseille UnivAbstract 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.https://doi.org/10.1038/s41598-017-04064-2 |
| spellingShingle | Elodie Foulquier Anne Galinier YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars Scientific Reports |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41598-017-04064-2 |
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