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A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120
Indole, as a signal molecule, is involved in multiple physiological behavior including biofilm formation, antibiotic resistance and virulence. In this study, we demonstrated that indole was involved in iron deficient and H(2)O(2) stress response in Muricauda olearia Th120. Transcriptome analysis sho...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5484670/ https://www.ncbi.nlm.nih.gov/pubmed/28652609 http://dx.doi.org/10.1038/s41598-017-04606-8 |
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author | Wang, Yan Li, Hui Cui, Xinxin Zhang, Xiao-Hua |
author_facet | Wang, Yan Li, Hui Cui, Xinxin Zhang, Xiao-Hua |
author_sort | Wang, Yan |
collection | PubMed |
description | Indole, as a signal molecule, is involved in multiple physiological behavior including biofilm formation, antibiotic resistance and virulence. In this study, we demonstrated that indole was involved in iron deficient and H(2)O(2) stress response in Muricauda olearia Th120. Transcriptome analysis showed that totally 206 genes were regulated by exogenous indole. Besides, momL-suf gene cluster, consisting of quorum quenching enzyme coding gene momL and iron-sulfur biosynthetic genes suf, were involved in indole-induced stress response pathway. The result indicated that indole not only up-regulated momL-suf gene cluster, but also enhanced the MomL secretion and the growth rates of MomL-bearing strains in H(2)O(2) stress and iron deficient culture conditions. Co-incubation of M. olearia Th120 and Pectobacterium carotovorum subsp. carotovorum under H(2)O(2) condition revealed that M. olearia Th120 bearing MomL possessed an increased competitive advantage, whereas its competitor had a reduced survival. The phenomenon that quorum quenching enzyme is triggered by stress factor has been rarely reported. The study also opens a new clue to explore the indole function towards quorum quenching factor in bacteria. |
format | Online Article Text |
id | pubmed-5484670 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54846702017-06-30 A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 Wang, Yan Li, Hui Cui, Xinxin Zhang, Xiao-Hua Sci Rep Article Indole, as a signal molecule, is involved in multiple physiological behavior including biofilm formation, antibiotic resistance and virulence. In this study, we demonstrated that indole was involved in iron deficient and H(2)O(2) stress response in Muricauda olearia Th120. Transcriptome analysis showed that totally 206 genes were regulated by exogenous indole. Besides, momL-suf gene cluster, consisting of quorum quenching enzyme coding gene momL and iron-sulfur biosynthetic genes suf, were involved in indole-induced stress response pathway. The result indicated that indole not only up-regulated momL-suf gene cluster, but also enhanced the MomL secretion and the growth rates of MomL-bearing strains in H(2)O(2) stress and iron deficient culture conditions. Co-incubation of M. olearia Th120 and Pectobacterium carotovorum subsp. carotovorum under H(2)O(2) condition revealed that M. olearia Th120 bearing MomL possessed an increased competitive advantage, whereas its competitor had a reduced survival. The phenomenon that quorum quenching enzyme is triggered by stress factor has been rarely reported. The study also opens a new clue to explore the indole function towards quorum quenching factor in bacteria. Nature Publishing Group UK 2017-06-26 /pmc/articles/PMC5484670/ /pubmed/28652609 http://dx.doi.org/10.1038/s41598-017-04606-8 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Wang, Yan Li, Hui Cui, Xinxin Zhang, Xiao-Hua A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 |
title | A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 |
title_full | A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 |
title_fullStr | A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 |
title_full_unstemmed | A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 |
title_short | A novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme MomL and iron-sulfur cluster in Muricauda olearia Th120 |
title_sort | novel stress response mechanism, triggered by indole, involved in quorum quenching enzyme moml and iron-sulfur cluster in muricauda olearia th120 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5484670/ https://www.ncbi.nlm.nih.gov/pubmed/28652609 http://dx.doi.org/10.1038/s41598-017-04606-8 |
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