Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation
Quorum sensing (QS) promotes in situ extracellular enzyme (EE) activity via the exogenous signal N-acylhomoserine lactone (AHL), which facilitates marine particle degradation, but the species that engage in this regulatory mechanism remain unclear. Here, we obtained AHL-producing and AHL-degrading s...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-01-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2018.03304/full |
| _version_ | 1811290750337417216 |
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| author | Ying Su Ying Su Kaihao Tang Jiwen Liu Jiwen Liu Yan Wang Yan Wang Yanfen Zheng Xiao-Hua Zhang Xiao-Hua Zhang |
| author_facet | Ying Su Ying Su Kaihao Tang Jiwen Liu Jiwen Liu Yan Wang Yan Wang Yanfen Zheng Xiao-Hua Zhang Xiao-Hua Zhang |
| author_sort | Ying Su |
| collection | DOAJ |
| description | Quorum sensing (QS) promotes in situ extracellular enzyme (EE) activity via the exogenous signal N-acylhomoserine lactone (AHL), which facilitates marine particle degradation, but the species that engage in this regulatory mechanism remain unclear. Here, we obtained AHL-producing and AHL-degrading strains from marine particles. The strain Ruegeria mobilis Rm01 of the Roseobacter group (RBG), which was capable of both AHL producing and degrading, was chosen to represent these strains. We demonstrated that Rm01 possessed a complex QS network comprising AHL-based QS and quorum quenching (QQ) systems and autoinducer-2 (AI-2) perception system. Rm01 was able to respond to multiple exogenous QS signals through the QS network. By applying self-generated AHLs and non-self-generated AHLs and AI-2 QS signal molecules, we modulated biofilm formation and lipase production in Rm01, which reflected the coordination of bacterial metabolism with that of other species via eavesdropping on exogenous QS signals. These results suggest that R. mobilis might be one of the participators that could regulate EE activities by responding to QS signals in marine particles. |
| first_indexed | 2024-04-13T04:18:08Z |
| format | Article |
| id | doaj.art-fa77152e3a934f5184ce066282100be9 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-04-13T04:18:08Z |
| publishDate | 2019-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-fa77152e3a934f5184ce066282100be92022-12-22T03:02:55ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2019-01-01910.3389/fmicb.2018.03304398963Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm FormationYing Su0Ying Su1Kaihao Tang2Jiwen Liu3Jiwen Liu4Yan Wang5Yan Wang6Yanfen Zheng7Xiao-Hua Zhang8Xiao-Hua Zhang9College of Marine Life Science, Ocean University of China, Qingdao, ChinaWeifang Engineering Vocational College, Weifang, ChinaCollege of Marine Life Science, Ocean University of China, Qingdao, ChinaCollege of Marine Life Science, Ocean University of China, Qingdao, ChinaLaboratory for Marine Ecology and Environmental Science, Qingdao National Laboratory for Marine Science and Technology, Qingdao, ChinaCollege of Marine Life Science, Ocean University of China, Qingdao, ChinaLaboratory for Marine Ecology and Environmental Science, Qingdao National Laboratory for Marine Science and Technology, Qingdao, ChinaCollege of Marine Life Science, Ocean University of China, Qingdao, ChinaCollege of Marine Life Science, Ocean University of China, Qingdao, ChinaLaboratory for Marine Ecology and Environmental Science, Qingdao National Laboratory for Marine Science and Technology, Qingdao, ChinaQuorum sensing (QS) promotes in situ extracellular enzyme (EE) activity via the exogenous signal N-acylhomoserine lactone (AHL), which facilitates marine particle degradation, but the species that engage in this regulatory mechanism remain unclear. Here, we obtained AHL-producing and AHL-degrading strains from marine particles. The strain Ruegeria mobilis Rm01 of the Roseobacter group (RBG), which was capable of both AHL producing and degrading, was chosen to represent these strains. We demonstrated that Rm01 possessed a complex QS network comprising AHL-based QS and quorum quenching (QQ) systems and autoinducer-2 (AI-2) perception system. Rm01 was able to respond to multiple exogenous QS signals through the QS network. By applying self-generated AHLs and non-self-generated AHLs and AI-2 QS signal molecules, we modulated biofilm formation and lipase production in Rm01, which reflected the coordination of bacterial metabolism with that of other species via eavesdropping on exogenous QS signals. These results suggest that R. mobilis might be one of the participators that could regulate EE activities by responding to QS signals in marine particles.https://www.frontiersin.org/article/10.3389/fmicb.2018.03304/fullmarine particlesquorum sensingquorum quenchingRuegeria mobilisbiofilm formationextracellular enzyme |
| spellingShingle | Ying Su Ying Su Kaihao Tang Jiwen Liu Jiwen Liu Yan Wang Yan Wang Yanfen Zheng Xiao-Hua Zhang Xiao-Hua Zhang Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation Frontiers in Microbiology marine particles quorum sensing quorum quenching Ruegeria mobilis biofilm formation extracellular enzyme |
| title | Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation |
| title_full | Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation |
| title_fullStr | Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation |
| title_full_unstemmed | Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation |
| title_short | Quorum Sensing System of Ruegeria mobilis Rm01 Controls Lipase and Biofilm Formation |
| title_sort | quorum sensing system of ruegeria mobilis rm01 controls lipase and biofilm formation |
| topic | marine particles quorum sensing quorum quenching Ruegeria mobilis biofilm formation extracellular enzyme |
| url | https://www.frontiersin.org/article/10.3389/fmicb.2018.03304/full |
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