{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["171(2)"],"submitter":["Bagchi S"],"pubmed_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 <i>Mycobacterium tuberculosis</i>. 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 <i>M. tuberculosis</i> were manipulated by overexpressing a c-di-GMP synthesizing enzyme <i>ydeH</i> and a degrading enzyme <i>rv1357c</i>. We demonstrate that overexpression of <i>ydeH</i> lowers growth of the bacterium "],"journal":["Microbiology (Reading, England)"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12282275"],"repository":["biostudies-literature"],"pubmed_title":["Crosstalk between cyclic-di-guanosine monophosphate and the sensor kinase MtrB regulates MtrA-dependent genes, bacterial growth, biofilm formation and lysosomal trafficking of &lt;i&gt;Mycobacterium tuberculosis&lt;/i&gt;."],"pmcid":["PMC12282275"],"pubmed_authors":["Mal S","Kundu M","Basu J","Sharma AK","Bagchi S"],"additional_accession":[]},"is_claimable":false,"name":"Crosstalk between cyclic-di-guanosine monophosphate and the sensor kinase MtrB regulates MtrA-dependent genes, bacterial growth, biofilm formation and lysosomal trafficking of &lt;i&gt;Mycobacterium tuberculosis&lt;/i&gt;.","description":"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 <i>Mycobacterium tuberculosis</i>. 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 <i>M. tuberculosis</i> were manipulated by overexpressing a c-di-GMP synthesizing enzyme <i>ydeH</i> and a degrading enzyme <i>rv1357c</i>. We demonstrate that overexpression of <i>ydeH</i> lowers growth of the bacterium ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-03-31T10:42:32.277Z","creation":"2025-08-24T03:08:52.301Z"},"accession":"S-EPMC12282275","cross_references":{"pubmed":["39918987"],"doi":["10.1099/mic.0.001532"]}}