2015
DOI: 10.7150/ijbs.11797
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Functional Analysis of a c-di-AMP-specific Phosphodiesterase MsPDE from Mycobacterium smegmatis

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,… Show more

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Cited by 53 publications
(90 citation statements)
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“…S. pneumoniae produces a homolog of DhhP named Pde2, which can hydrolyze c-di-AMP and pApA as well as 3′-phosphoadenosine-5′-phosphate (pAp) to AMP and is essential for pathogenesis (24, 29). The Mycobacterium tuberculosis and Mycobacterium smegmatis homologs, MtbPDE and MtPDE, respectively, have been shown to degrade both c-di-AMP and pApA (3033). A third class of c-di-AMP PDE found in c-di-AMP-producing microorganisms is an HD-domain containing enzyme (17, 34).…”
Section: Introductionmentioning
confidence: 99%
“…S. pneumoniae produces a homolog of DhhP named Pde2, which can hydrolyze c-di-AMP and pApA as well as 3′-phosphoadenosine-5′-phosphate (pAp) to AMP and is essential for pathogenesis (24, 29). The Mycobacterium tuberculosis and Mycobacterium smegmatis homologs, MtbPDE and MtPDE, respectively, have been shown to degrade both c-di-AMP and pApA (3033). A third class of c-di-AMP PDE found in c-di-AMP-producing microorganisms is an HD-domain containing enzyme (17, 34).…”
Section: Introductionmentioning
confidence: 99%
“…Thus far, these proteins have been characterized in S. pneumoniae, B. burgdorferi, M. tuberculosis , and M. smegmatis [3,7,9,10]. Among those species, only S. pneumoniae also encodes a GdpP homolog, whereas others encode only DhhP.…”
Section: Introductionmentioning
confidence: 99%
“…Most characterized DhhP proteins degrade both c-di-AMP and 5’-pApA into AMP, as well as c-di-GMP and 5’-pGpG into GMP. Nevertheless, in M. smegmatis , the catalytic efficiency (k cat /k M ) is approximately 200-fold higher for c-di-AMP than for c-di-GMP, indicating that c-di-AMP is the much preferred substrate [10]. Additionally, at least the M. tuberculosis homolog has also been characterized as an NrnA with exonuclease activity on short single stranded nucleic acids, as well as phosphatase activity on pAp [5].…”
Section: Introductionmentioning
confidence: 99%
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“…111 High c-di-AMP levels have also been shown to trigger stringent response resulting in an increase in the levels of the alarmone (p)ppGpp in S. aureus. 18 Exogenously added c-di-AMP enhanced B. subtilis sporulation 120 while overexpression of MsDisA in M. smegmatis (implying increased c-di-AMP levels) resulted in minute colonies 121 (Fig. 12).…”
Section: Inhibitors Of C-di-gmpmentioning
confidence: 99%