Cited by 109Bacterial Genetics and BiotechnologyAntimicrobial Resistance in StaphylococcusBiochemical and Molecular Research

The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus

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Schuster, Christopher F., Bellows, Lauren E., Tosi, Tommaso, Campeotto, Ivan, Corrigan, Rebecca M., Freemont, Paul, Gründling, Angelika·2016·Science Signaling

Abstract

The second messenger c-di-AMP binds to and inhibits a component of a transporter that helps bacterial cells adapt to osmotic stress.

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Crossref · 10.1126/scisignal.aaf7279

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  • Increased c-di-AMP inhibits compatible solute uptake by the Opu-family proteins.

    “Furthermore, increased c-di-AMP inhibits compatible solute uptake by the Opu-family proteins (35, 46).”

    From A Central Role for Magnesium Homeostasis during Adaptation to Osmotic Stress (2022) · cites this paper as [35]

    The Results report reduced carnitine uptake at early time points in a Staphylococcus aureus strain with elevated c-di-AMP, and the Discussion identifies OpuC as the relevant transporter. The paper does not establish inhibition across Opu-family proteins or compatible solutes generally; it says OpuC was the only osmoprotectant uptake system identified as a c-di-AMP target. (LLM, conf=0.88)

    Experimental — accuracy not yet measured
  • Cyclic di-AMP has been implicated in growth under osmotic stress due to its central role in coordinating K+ homeostasis.

    “Cyclic di-AMP has been implicated in growth under osmotic stress due to its central role in coordinating K+ homeostasis (26, 35, 36).”
  • The pgpH gdpP double mutant was not rescued by glycine betaine.

    “Interestingly, and consistent with the established inhibition of compatible solute import by c-di-AMP (35, 39, 40), the pgpH gdpP double mutant was not rescued by GB (Fig. S4B).”

    From A Central Role for Magnesium Homeostasis during Adaptation to Osmotic Stress (2022) · cites this paper as [35]

    The citation supports the preceding background point about c-di-AMP inhibiting compatible-solute uptake, not the citing paper’s observation that its pgpH gdpP double mutant was not rescued by glycine betaine; that observation points to Fig. S4B. The source’s Results section reports reduced carnitine uptake in a ΔgdpP strain, but does not address glycine-betaine rescue of a pgpH gdpP double mutant. (LLM, conf=0.78)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 77

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Cited by

Sorted by citations

Authors
Schuster, C. F., Bellows, L. E., Tosi, T., Campeotto, I., Corrigan, R. M., Freemont, P., & Gründling, A.
Affiliations
Imperial College London (GB)
Corresponding author
  • Schuster, Christopher F.
  • Bellows, Lauren E.
  • Gründling, Angelika
Venue
Science Signaling
Published
2016-08-16
Volume
9
Issue
441
Pages
ra81-ra81
ISSN
  • 1937-9145 (ISSN-L)
  • 1945-0877
OpenAlex
W2507323902
Cited by
109
References
0
Citations by year
2026: 6 · 2025: 7 · 2024: 13 · 2023: 17 · 2022: 10 · 2021: 8 · 2020: 15 · 2019: 14 · 2018: 7 · 2017: 9 · 2016: 3
FWCI
8.89
Type
journal article
Language
en
Open access
Locations
  • Science Signaling (publishedVersion)
  • PubMed (publishedVersion)
  • White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • Nottingham Trent University's Institutional Repository (Nottingham Trent Repository) (submittedVersion)
  • Spiral (Imperial College London) (submittedVersion)
Funders
  • European Research Council (260371)
  • Wellcome Trust (100289)
  • Deutsche Forschungsgemeinschaft (DFG) (SCHU 3159/1-1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords
c-di-AMP, Staphylococcus aureus, osmotic stress, osmolytes, carnitine uptake, potassium uptake, second messenger signaling, ATPase, CBS domain, protein inhibition, crystal structure
MeSH terms
Protein Domains, Bacterial Proteins, Carnitine, Osmotic Pressure, Staphylococcus aureus, Dinucleoside Phosphates, Second Messenger Systems, Crystallography, X-Ray, ATP-Binding Cassette Transporters

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