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Diguanylate Cyclase and Phosphodiesterase Interact To Maintain the Specificity of Cyclic di-GMP Signaling in the Regulation of Antibiotic Synthesis in Lysobacter enzymogenes

文献类型： 外文期刊

作者： Xu, Gaoge 1 ; Zhou, Lichuan 2 ; Qian, Guoliang 3 ; Liu, Fengquan 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Plant Protect, Jiangsu Key Lab Food Qual & Safety, Minist Sci & Technol,State Key Lab Cultivat Base, Nanjing, Peoples R China

2.Jiangsu Acad Agr Sci, Informat Ctr, Nanjing, Peoples R China

3.Nanjing Agr Univ, Coll Plant Protect, Nanjing, Peoples R China

4.Hainan Univ, Coll Plant Protect, Minist Educ, Key Lab Green Prevent & Control Trop Plant Dis &, Haikou, Hainan, Peoples R China

关键词： c-di-GMP; signaling specificity; local c-di-GMP signaling; HSAF; diguanylate cyclase

期刊名称：APPLIED AND ENVIRONMENTAL MICROBIOLOGY （ 影响因子：5.005； 五年影响因子：5.632 ）

ISSN： 0099-2240

年卷期： 2022 年 88 卷 2 期

页码：

收录情况： SCI

摘要： Cyclic dimeric GMP (c-di-GMP) is a universal second messenger in bacteria. A large number of c-di-GMP-related diguanylate cyclases (DGCs), phosphodiesterases (PDEs), and effectors are responsible for the complexity and dynamics of c-di-GMP signaling. Some of these components employ various methods to avoid undesired cross talk to maintain signaling specificity. The synthesis of the antibiotic HSAF (heat-stable antifungal factor) in Lysobacter enzymogenes is regulated by a specific c-di-GMP signaling pathway that includes a PDE, LchP, and a c-di-GMP effector, Clp (also a transcriptional regulator). In the present study, from among 19 DGCs, we identified a diguanylate cyclase, LchD, that participates in this pathway. Subsequent investigation indicates that LchD and LchP physically interact and that the catalytic center of LchD is required for both the formation of the LchD-LchP complex and HSAF production. All the detected phenotypes support that LchD and LchP display local c-di-GMP signaling to regulate HSAF biosynthesis. Although direct evidence is lacking, our investigation, which shows that the interaction between a DGC and a PDE maintains the specificity of c-di-GMP signaling, suggests the possibility of the existence of local c-di-GMP pools in bacteria. IMPORTANCE Cyclic dimeric GMP (c-di-GMP) is a universal second messenger in bacteria. The signaling of c-di-GMP is complex and dynamic, and it is mediated by a large number of components, including c-di-GMP synthases (diguanylate cyclases [DGCs]), c-di-GMP-degrading enzymes (phosphodiesterases [PDEs]), and c-di-GMP effectors. These components deploy various methods to avoid undesired cross talk to maintain signaling specificity. In the present study, we identified a DGC that interacted with a PDE to specifically regulate antibiotic biosynthesis in L. enzymogenes. We provide direct evidence to show that the DGC and PDE form a complex and also indirect evidence to argue that they may balance a local c-di-GMP pool to control antibiotic production. These results represent an important finding regarding the mechanism of a DGC and PDE pair to control the expression of specific c-diGMP signaling pathways.

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