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• W2550542562 endingPage "26986" @default.
• W2550542562 startingPage "26970" @default.
• W2550542562 abstract "Nucleotide signaling networks are key to facilitate alterations in gene expression, protein function, and enzyme activity in response to diverse stimuli. Cyclic di-adenosine monophosphate (c-di-AMP) is an important secondary messenger molecule produced by the human pathogen Staphylococcus aureus and is involved in regulating a number of physiological processes including potassium transport. S. aureus must ensure tight control over its cellular levels as both high levels of the dinucleotide and its absence result in a number of detrimental phenotypes. Here we show that in addition to the membrane-bound Asp-His-His and Asp-His-His-associated (DHH/DHHA1) domain-containing phosphodiesterase (PDE) GdpP, S. aureus produces a second cytoplasmic DHH/DHHA1 PDE Pde2. Although capable of hydrolyzing c-di-AMP, Pde2 preferentially converts linear 5'-phosphadenylyl-adenosine (pApA) to AMP. Using a pde2 mutant strain, pApA was detected for the first time in S. aureus, leading us to speculate that this dinucleotide may have a regulatory role under certain conditions. Moreover, pApA is involved in a feedback inhibition loop that limits GdpP-dependent c-di-AMP hydrolysis. Another protein linked to the regulation of c-di-AMP levels in bacteria is the predicted regulator protein YbbR. Here, it is shown that a ybbR mutant S. aureus strain has increased acid sensitivity that can be bypassed by the acquisition of mutations in a number of genes, including the gene coding for the diadenylate cyclase DacA. We further show that c-di-AMP levels are slightly elevated in the ybbR suppressor strains tested as compared with the wild-type strain. With this, we not only identified a new role for YbbR in acid stress resistance in S. aureus but also provide further insight into how c-di-AMP levels impact acid tolerance in this organism." @default.
• W2550542562 created "2016-11-30" @default.
• W2550542562 creator A5051742131 @default.
• W2550542562 creator A5077663778 @default.
• W2550542562 creator A5079560105 @default.
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• W2550542562 creator A5086400698 @default.
• W2550542562 date "2016-12-01" @default.
• W2550542562 modified "2023-10-12" @default.
• W2550542562 title "New Insights into the Cyclic Di-adenosine Monophosphate (c-di-AMP) Degradation Pathway and the Requirement of the Cyclic Dinucleotide for Acid Stress Resistance in Staphylococcus aureus" @default.
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• W2550542562 doi "https://doi.org/10.1074/jbc.m116.747709" @default.
• W2550542562 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5207132" @default.
• W2550542562 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27834680" @default.
• W2550542562 hasPublicationYear "2016" @default.
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