ArticleThe Journal of biological chemistry2013
Cyclic di-AMP homeostasis in bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.
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135 citing papers in PubMed, 197 citations in OpenAlex.
- Mislocalization of PBPs inMicrobiology spectrum · 2026Article
- Cyclic di-AMP signaling and regulation inmSphere · 2026Review
- Post-translational modifications of GlmR integrate metabolic and stress signals to maintain cell envelope homeostasis in Bacillus subtilis.PLoS genetics · 2026Article
- Cyclic di-adenosine monophosphate as a potential regulator of sporulation and solventogenesis in Clostridium beijerinckii: a hypothesis.World journal of microbiology & biotechnology · 2026Review
- Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025Article
- TrkA ofMicrobiology (Reading, England) · 2025Article
- Cyclic-di-AMP modulates cellular turgor in response to defects in bacterial cell wall synthesis.Nature microbiology · 2025Article
- Article
- Membrane-embedded CdaA is required for efficient synthesis of second messenger cyclic di-AMP.Communications biology · 2024Article
- A multi-epitope subunit vaccine providing broad cross-protection against diverse serotypes of Streptococcus suis.NPJ vaccines · 2024Article
- Article
- Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024Review
- Review
- Reversible conjugation of a CBASS nucleotide cyclase regulates bacterial immune response to phage infection.Nature microbiology · 2024Article
- A small step towards an important goal: fragment screen of the c-di-AMP-synthesizing enzyme CdaA.Acta crystallographica. Section D, Structural biology · 2024Article
- Structural insights into the regulation, ligand recognition, and oligomerization of bacterial STING.Nature communications · 2023Article
- Nucleotides as Bacterial Second Messengers.Molecules (Basel, Switzerland) · 2023Review
- Synthesis and degradation of the cyclic dinucleotide messenger c-di-AMP in the hyperthermophilic archaeon Pyrococcus yayanosii.Protein science : a publication of the Protein Society · 2023Article
- Cyclic di-AMP traps proton-coupled KNature communications · 2023Article
- All DACs in a Row: Domain Architectures of Bacterial and Archaeal Diadenylate Cyclases.Journal of bacteriology · 2023Review
75 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of the Gram-positive soil bacterium Bacillus subtilis encodes three potential diadenylate cyclases that may synthesize the signaling nucleotide cyclic di-AMP (c-di-AMP). These enzymes are expressed under different conditions in different cell compartments, and they localize to distinct positions in the cell. Here we demonstrate the diadenylate cyclase activity of the so far uncharacterized enzymes CdaA (previously known as YbbP) and CdaS (YojJ). Our work confirms that c-di-AMP is essential for the growth of B. subtilis and shows that an excess of the molecule is also harmful for the bacteria. Several lines of evidence suggest that the diadenylate cyclase CdaA is part of the conserved essential cda-glm module involved in cell wall metabolism. In contrast, the CdaS enzyme seems to provide c-di-AMP for spores. Accumulation of large amounts of c-di-AMP impairs the growth of B. subtilis and results in the formation of aberrant curly cells. This phenotype can be partially suppressed by elevated concentrations of magnesium. These observations suggest that c-di-AMP interferes with the peptidoglycan synthesis machinery. The activity of the diadenylate cyclases is controlled by distinct molecular mechanisms. CdaA is stimulated by a regulatory interaction with the CdaR (YbbR) protein. In contrast, the activity of CdaS seems to be intrinsically restricted, and a single amino acid substitution is sufficient to drastically increase the activity of the enzyme. Taken together, our results support the idea of an important role for c-di-AMP in B. subtilis and suggest that the levels of the nucleotide have to be tightly controlled.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.