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Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae
The highly conserved ATP-dependent Lon protease plays important roles in diverse biological processes. The lon gene is usually nonessential for viability; however, lon mutants of several bacterial species, although viable, exhibit cellular defects. Here, we show that a lack of Lon protease causes pl...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8443046/ https://www.ncbi.nlm.nih.gov/pubmed/34525127 http://dx.doi.org/10.1371/journal.pone.0257257 |
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author | Goo, Eunhye Hwang, Ingyu |
author_facet | Goo, Eunhye Hwang, Ingyu |
author_sort | Goo, Eunhye |
collection | PubMed |
description | The highly conserved ATP-dependent Lon protease plays important roles in diverse biological processes. The lon gene is usually nonessential for viability; however, lon mutants of several bacterial species, although viable, exhibit cellular defects. Here, we show that a lack of Lon protease causes pleiotropic effects in the rice pathogen Burkholderia glumae. The null mutation of lon produced three colony types, big (BLONB), normal (BLONN), and small (BLONS), in Luria–Bertani (LB) medium. Colonies of the BLONB and BLONN types were re-segregated upon subculture, while those of the BLONS type were too small to manipulate. The BLONN type was chosen for further studies, as only this type was fully genetically complemented. BLONN-type cells did not reach the maximum growth capacity, and their population decreased drastically after the stationary phase in LB medium. BLONN-type cells were defective in the biosynthesis of quorum sensing (QS) signals and exhibited reduced oxalate biosynthetic activity, causing environmental alkaline toxicity and population collapse. Addition of excessive N-octanoyl-homoserine lactone (C8-HSL) to BLONN-type cell cultures did not fully restore oxalate biosynthesis, suggesting that the decrease in oxalate biosynthesis in BLONN-type cells was not due to insufficient C8-HSL. Co-expression of lon and tofR in Escherichia coli suggested that Lon negatively affects the TofR level in a C8-HSL-dependent manner. Lon protease interacted with the oxalate biosynthetic enzymes, ObcA and ObcB, indicating potential roles for the oxalate biosynthetic activity. These results suggest that Lon protease influences colony morphology, growth, QS system, and oxalate biosynthesis in B. glumae. |
format | Online Article Text |
id | pubmed-8443046 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-84430462021-09-16 Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae Goo, Eunhye Hwang, Ingyu PLoS One Research Article The highly conserved ATP-dependent Lon protease plays important roles in diverse biological processes. The lon gene is usually nonessential for viability; however, lon mutants of several bacterial species, although viable, exhibit cellular defects. Here, we show that a lack of Lon protease causes pleiotropic effects in the rice pathogen Burkholderia glumae. The null mutation of lon produced three colony types, big (BLONB), normal (BLONN), and small (BLONS), in Luria–Bertani (LB) medium. Colonies of the BLONB and BLONN types were re-segregated upon subculture, while those of the BLONS type were too small to manipulate. The BLONN type was chosen for further studies, as only this type was fully genetically complemented. BLONN-type cells did not reach the maximum growth capacity, and their population decreased drastically after the stationary phase in LB medium. BLONN-type cells were defective in the biosynthesis of quorum sensing (QS) signals and exhibited reduced oxalate biosynthetic activity, causing environmental alkaline toxicity and population collapse. Addition of excessive N-octanoyl-homoserine lactone (C8-HSL) to BLONN-type cell cultures did not fully restore oxalate biosynthesis, suggesting that the decrease in oxalate biosynthesis in BLONN-type cells was not due to insufficient C8-HSL. Co-expression of lon and tofR in Escherichia coli suggested that Lon negatively affects the TofR level in a C8-HSL-dependent manner. Lon protease interacted with the oxalate biosynthetic enzymes, ObcA and ObcB, indicating potential roles for the oxalate biosynthetic activity. These results suggest that Lon protease influences colony morphology, growth, QS system, and oxalate biosynthesis in B. glumae. Public Library of Science 2021-09-15 /pmc/articles/PMC8443046/ /pubmed/34525127 http://dx.doi.org/10.1371/journal.pone.0257257 Text en © 2021 Goo, Hwang https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Goo, Eunhye Hwang, Ingyu Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae |
title | Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae |
title_full | Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae |
title_fullStr | Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae |
title_full_unstemmed | Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae |
title_short | Essential roles of Lon protease in the morpho-physiological traits of the rice pathogen Burkholderia glumae |
title_sort | essential roles of lon protease in the morpho-physiological traits of the rice pathogen burkholderia glumae |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8443046/ https://www.ncbi.nlm.nih.gov/pubmed/34525127 http://dx.doi.org/10.1371/journal.pone.0257257 |
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