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

Autor:	Schuster CF; Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK., Bellows LE; Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK., Tosi T; Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK., Campeotto I; Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK., Corrigan RM; Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK., Freemont P; Section of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK., Gründling A; Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Jazyk:	angličtina
Zdroj:	Science signaling [Sci Signal] 2016 Aug 16; Vol. 9 (441), pp. ra81. Date of Electronic Publication: 2016 Aug 16.
DOI:	10.1126/scisignal.aaf7279
Abstrakt:	Staphylococcus aureus is an important opportunistic human pathogen that is highly resistant to osmotic stresses. To survive an increase in osmolarity, bacteria immediately take up potassium ions and small organic compounds known as compatible solutes. The second messenger cyclic diadenosine monophosphate (c-di-AMP) reduces the ability of bacteria to withstand osmotic stress by binding to and inhibiting several proteins that promote potassium uptake. We identified OpuCA, the adenosine triphosphatase (ATPase) component of an uptake system for the compatible solute carnitine, as a c-di-AMP target protein in S aureus and found that the LAC*ΔgdpP strain of S aureus, which overproduces c-di-AMP, showed reduced carnitine uptake. The paired cystathionine-β-synthase (CBS) domains of OpuCA bound to c-di-AMP, and a crystal structure revealed a putative binding pocket for c-di-AMP in the cleft between the two CBS domains. Thus, c-di-AMP inhibits osmoprotection through multiple mechanisms. Competing Interests: The authors do not have a conflict of interest to declare. (Copyright © 2016, American Association for the Advancement of Science.)
Databáze:	MEDLINE
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