TY - JOUR AB - 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 LACΔgdpP 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. AU - Schuster,C AU - Bellows,L AU - Tosi,T AU - Campeotto AU - Corrigan AU - Freemont,P AU - Grundling,A DO - 10.1126/scisignal.aaf7279 EP - 81 PY - 2016/// SN - 1945-0877 SP - 81 TI - The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus T2 - Science Signaling UR - http://dx.doi.org/10.1126/scisignal.aaf7279 UR - http://stke.sciencemag.org/cgi/reprint/sigtrans;9/441/ra81?ijkey=SZluRyjzK/0hw&keytype=ref&siteid=sigtrans UR - http://hdl.handle.net/10044/1/39084 VL - 9 ER -