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

ABSTRACT: 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 an

SUBMITTER: Xu G 

PROVIDER: S-EPMC8788788 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature