ArticleInternational journal of biological sciences2015
Functional Analysis of a c-di-AMP-specific Phosphodiesterase MsPDE from Mycobacterium smegmatis.
Article in International journal of biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 60 citations in OpenAlex.
- Altered abundance in cancer patients gut of diadenylate cyclase-encoding bacteria.Scientific reports · 2026Article
- The c-di-AMP binding protein NadD from Mesomycoplasma ovipneumoniae functions as a phosphodiesterase that inhibits host inflammatory responses.Veterinary research · 2026Article
- Exploring the evolutionary divergence of cyclic di-nucleotide signaling in diverse mycobacterial species.Archives of microbiology · 2026Article
- Functional analyses of bacterial NanoRNase B proteins reveals defining features of this enzyme family.Nucleic acids research · 2025Article
- Functional Differentiation and Regulatory Mechanisms of Ferrochelatases HemH1 and HemH2 inInternational journal of molecular sciences · 2025Article
- An HPLC-based Assay to Study the Activity of Cyclic Diadenosine Monophosphate (C-di-AMP) Synthase DisA fromBio-protocol · 2024Article
- Bacillus subtilis NrnB is expressed during sporulation and acts as a unique 3'-5' exonuclease.Nucleic acids research · 2023Article
- Elucidating the role of c-di-AMP inHeliyon · 2023Article
- All DACs in a Row: Domain Architectures of Bacterial and Archaeal Diadenylate Cyclases.Journal of bacteriology · 2023Review
- C-di-AMP Is a Second Messenger inMicroorganisms · 2023Article
- Sub-operon promoter arrangement ofJournal of biosciences · 2023Article
- c-di-AMP signaling plays important role in determining antibiotic tolerance phenotypes of Mycobacterium smegmatis.Scientific reports · 2022Article
- NrnA Is a Linear Dinucleotide Phosphodiesterase with Limited Function in Cyclic Dinucleotide Metabolism in Listeria monocytogenes.Journal of bacteriology · 2022Article
- The role of bacterial cyclic di-adenosine monophosphate in the host immune response.Frontiers in microbiology · 2022Review
- Cyclic di-AMP as endogenous adjuvant enhanced BCG-induced trained immunity and protection againstFrontiers in immunology · 2022Article
- Cyclic-di-AMP Phosphodiesterase Elicits Protective Immune Responses AgainstFrontiers in cellular and infection microbiology · 2022Article
- c-di-AMP Accumulation Regulates Growth, Metabolism, and Immunogenicity ofFrontiers in microbiology · 2022Article
- A Luminescence-Based Coupled Enzyme Assay Enables High-Throughput Quantification of the Bacterial Second Messenger 3'3'-Cyclic-Di-AMP.Chembiochem : a European journal of chemical biology · 2021Article
- Ways to control harmful biofilms: prevention, inhibition, and eradication.Critical reviews in microbiology · 2021Review
- Assessment of Diadenylate Cyclase and c-di-AMP-phosphodiesterase Activities Using Thin-layer and Ion Exchange Chromatography.Bio-protocol · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclic di‑AMP (c-di-AMP) is a second signaling molecule involved in the regulation of bacterial physiological processes and interaction between pathogen and host. However, the regulatory network mediated by c-di-AMP in Mycobacterium remains obscure. In M. smegmatis, a diadenylate cyclase (DAC) was reported recently, but there is still no investigation on c-di-AMP phosphodiesterase (PDE). Here, we provide a systematic study on signaling mechanism of c-di-AMP PDE in M. smegmatis. Based on our enzymatic analysis, MsPDE (MSMEG_2630), which contained a DHH-DHHA1 domain, displayed a 200-fold higher hydrolytic efficiency (kcat /Km ) to c-di-AMP than to c-di-GMP. MsPDE was capable of converting c-di-AMP to pApA and AMP, and hydrolyzing pApA to AMP. Site-directed mutations in DHH and DHHA1 revealed that DHH domain was critical for the phosphodiesterase activity. To explore the regulatory role of c-di-AMP in vivo, we constructed the mspde mutant (Δmspde) and found that deficiency of MsPDE significantly enhanced intracellular C12-C20 fatty acid accumulation. Deficiency of DAC in many bacteria results in cell death. However, we acquired the M. smegmatis strain with DAC gene disrupted (ΔmsdisA) by homologous recombination approach. Deletion of msdisA reduced bacterial C12-C20 fatty acids production but scarcely affected bacterial survival. We also provided evidences that superfluous c-di-AMP in M. smegmatis could lead to abnormal colonial morphology. Collectively, our results indicate that MsPDE is a functional c-di-AMP-specific phosphodiesterase both in vitro and in vivo. Our study also expands the regulatory network mediated by c-di-AMP in M. smegmatis.
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