Cyclic Di-adenosine Monophosphate Regulates Metabolism and Growth in the Oral Commensal Streptococcus mitis
| العنوان: | Cyclic Di-adenosine Monophosphate Regulates Metabolism and Growth in the Oral Commensal Streptococcus mitis |
|---|---|
| المؤلفون: | Ali-Oddin Naemi, Krystyna Anna Liskiewicz, Thomas Küntziger, Fernanda Cristina Petersen, Roger Simm, Fedor Kryuchkov, Hans Christian Aasheim, Gro Herredsvela Rørvik |
| المصدر: | Microorganisms Volume 8 Issue 9 Microorganisms, Vol 8, Iss 1269, p 1269 (2020) |
| بيانات النشر: | Multidisciplinary Digital Publishing Institute, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Microbiology (medical), Adenosine monophosphate, growth, Mutant, Microbiology, Cyclase, diadenylate cyclase, 03 medical and health sciences, chemistry.chemical_compound, Virology, Streptococcus mitis, Extracellular, lcsh:QH301-705.5, 030304 developmental biology, 0303 health sciences, biology, 030306 microbiology, Phosphodiesterase, Metabolism, biology.organism_classification, c-di-AMP, lcsh:Biology (General), chemistry, Biochemistry, phosphodiesterase, metabolism, Intracellular |
| الوصف: | Cyclic di-adenosine monophosphate (c-di-AMP) has emerged as an important bacterial signaling molecule that functions both as an intracellular second messenger in bacterial cells and an extracellular ligand involved in bacteria-host cross-talk. In this study, we identify and characterize proteins involved in controlling the c-di-AMP concentration in the oral commensal and opportunistic pathogen Streptococcusmitis (S. mitis). We identified three known types of c-di-AMP turnover proteins in the genome of S. mitis CCUG31611: a CdaA-type diadenylate cyclase as well as GdpP-, and DhhP-type phosphodiesterases. Biochemical analyses of purified proteins demonstrated that CdaA synthesizes c-di-AMP from ATP whereas both phosphodiesterases can utilize c-di-AMP as well as the intermediary metabolite of c-di-AMP hydrolysis 5&prime phosphadenylyl-adenosine (pApA) as substrate to generate AMP, albeit at different catalytic efficiency. Using deletion mutants of each of the genes encoding c-di-AMP turnover proteins, we show by high resolution MS/MS that the intracellular concentration of c-di-AMP is increased in deletion mutants of the phosphodiesterases and non-detectable in the cdaA-mutant. We also detected pApA in mutants of the DhhP-type phosphodiesterase. Low and high levels of c-di-AMP were associated with longer and shorter chains of S. mitis, respectively indicating a role in regulation of cell division. The deletion mutant of the DhhP-type phosphodiesterase displayed slow growth and reduced rate of glucose metabolism. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 2076-2607 |
| DOI: | 10.3390/microorganisms8091269 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00292167ab1d5b3e64a99dab684229e1Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....00292167ab1d5b3e64a99dab684229e1 |
| قاعدة البيانات: | OpenAIRE |
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We also detected pApA in mutants of the DhhP-type phosphodiesterase. Low and high levels of c-di-AMP were associated with longer and shorter chains of S. mitis, respectively indicating a role in regulation of cell division. 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