Crosstalk between cyclic-di-guanosine monophosphate and the sensor kinase MtrB regulates MtrA-dependent genes, bacterial growth, biofilm formation and lysosomal trafficking of <i>Mycobacterium tuberculosis</i>.

ABSTRACT: Cyclic-di-guanosine monophosphate (c-di-GMP) plays an important role in bacterial signalling networks. C-di-GMP exerts a regulatory function through binding to diverse molecules that include transcription factors, riboswitches and sensor kinases (SKs), thereby regulating diverse processes. Here, we demonstrate the crosstalk between c-di-GMP and the SK MtrB of Mycobacterium tuberculosis. MtrB phosphorylates and regulates its cognate response regulator MtrA. C-di-GMP binds directly to the cytosolic domain of MtrB to inhibit its autophosphorylation. C-di-GMP levels in M. tuberculosis were manipulated by overexpressing a c-di-GMP synthesizing enzyme ydeH and a degrading enzyme rv1357c. We demonstrate that overexpression of ydeH lowers growth of the bacterium

SUBMITTER: Bagchi S 

PROVIDER: S-EPMC12282275 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature