Coordinated control of the type IV pili and c‐di‐GMP‐dependent antifungal antibiotic production in L ysobacter by the response regulator PilR
Autor: | Kangwen Xu, Danyu Shen, Nianda Yang, Mark Gomelsky, Shan-Ho Chou, Guoliang Qian |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
0106 biological sciences
0301 basic medicine Antifungal Agents Diguanylate cyclase activity Operon Soil Science Repressor Plant Science Lysobacter PilS‐PilR 01 natural sciences Models Biological 03 medical and health sciences Bacterial Proteins antibiotic biocontrol Phosphorylation Promoter Regions Genetic Molecular Biology Cyclic GMP biology Antifungal antibiotic c‐di‐GMP Escherichia coli Proteins Histidine kinase Original Articles biology.organism_classification Cell biology Response regulator 030104 developmental biology Fimbriae Bacterial biology.protein Diguanylate cyclase Original Article Phosphorus-Oxygen Lyases Agronomy and Crop Science 010606 plant biology & botany Signal Transduction Transcription Factors |
Zdroj: | Molecular Plant Pathology |
ISSN: | 1364-3703 1464-6722 |
Popis: | In the soil gammaproteobacterium Lysobacter enzymogenes, a natural fungal predator, the response regulator PilR controls type IV pili (T4P)‐mediated twitching motility as well as synthesis of the heat‐stable antifungal factor (HSAF). Earlier we showed that PilR acts via the second messenger, c‐di‐GMP; however, the mechanism remained unknown. Here, we describe how PilR, c‐di‐GMP signalling, and HSAF synthesis are connected. We screened genes for putative diguanylate cyclases (c‐di‐GMP synthases) and found that PilR binds to the promoter region of lchD and down‐regulates its transcription. The DNA‐binding affinity of PilR, and therefore its repressor function, are enhanced by phosphorylation by its cognate histidine kinase, PilS. The lchD gene product is a diguanylate cyclase, and the decrease in LchD levels shifts the ratio of c‐di‐GMP‐bound and c‐di‐GMP‐free transcription factor Clp, a key activator of the HSAF biosynthesis operon expression. Furthermore, Clp directly interacts with LchD and enhances its diguanylate cyclase activity. Therefore, the PilS–PilR two‐component system activates T4P‐motility while simultaneously decreasing c‐di‐GMP levels and promoting HSAF production via the highly specific LchD–c‐di‐GMP–Clp pathway. Coordinated increase in motility and secretion of the “long‐distance” antifungal weapon HSAF is expected to ensure safer grazing of L. enzymogenes on soil or plant surfaces, unimpeded by fungal competitors, or to facilitate bacterial preying on killed fungal cells. This study uncovered the mechanism of coregulated pili‐based motility and production of an antifungal antibiotic in L. enzymogenes, showcased the expanded range of functions of the PilS–PilR system, and highlighted exquisite specificity in c‐di‐GMP‐mediated circuits. PilR phosphorylation mediated by PilS down‐regulates lchD expression via DNA binding to lower c‐di‐GMP synthesis and thus accumulate c‐di‐GMP‐free Clp, which activates heat‐stable antifungal factor production via DNA binding. |
Databáze: | OpenAIRE |
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