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      Potassium Uptake Systems in Staphylococcus aureus: New Stories about Ancient Systems

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      Publication date (Electronic):
      Journal: mBio
      Publisher: American Society of Microbiology

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          ABSTRACT

          Staphylococcus aureus is a hardy organism that can survive high-salt conditions better than many other bacteria. This characteristic is thought to help S. aureus survive in the nares and on the skin of the human host and is used to selectively propagate and identify Staphylococcus species. However, the mechanism that allows S. aureus to tolerate such high-salt conditions is not well understood. A recent study in mBio by A. Price-Whelan et al. [mBio 4(4):e00407-13, 2013, doi:10.1128/mBio.00407-13] highlights the importance of potassium uptake in this process. This commentary provides a perspective of the study by Price-Whelan et al. as well as other recently reported work on potassium uptake and transport systems in S. aureus.

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          Cyclic di-AMP: another second messenger enters the fray.

          Angelika Gründling, Rebecca R. Corrigan (2013)
          Nucleotide signalling molecules contribute to the regulation of cellular pathways in all forms of life. In recent years, the discovery of new signalling molecules in bacteria and archaea, as well as the elucidation of the pathways they regulate, has brought insights into signalling mechanisms not only in bacterial and archaeal cells but also in eukaryotic host cells. Here, we provide an overview of the synthesis and regulation of cyclic di-AMP (c-di-AMP), one of the latest cyclic nucleotide second messengers to be discovered in bacteria. We also discuss the currently known receptor proteins and pathways that are directly or indirectly controlled by c-di-AMP, the domain structure of the enzymes involved in its production and degradation, and the recognition of c-di-AMP by the eukaryotic host.
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            The roles and regulation of potassium in bacteria.

            W V Epstein (2002)
            Potassium is the major intracellular cation in bacteria as well as in eucaryotic cells. Bacteria accumulate K+ by a number of different transport systems that vary in kinetics, energy coupling, and regulation. The Trk and Kdp systems of enteric organisms have been well studied and are found in many distantly related species. The Ktr system, resembling Trk in many ways, is also found in many bacteria. In most species two or more independent saturable K(+)-transport systems are present. The KefB and KefC type of system that is activated by treatment of cells with toxic electrophiles is the only specific K(+)-efflux system that has been well characterized. Pressure-activated channels of at least three types are found in bacteria; these represent nonspecific paths of efflux when turgor pressure is dangerously high. A close homolog of eucaryotic K+ channels is found in many bacteria, but its role remains obscure. K+ transporters are regulated both by ion concentrations and turgor. A very general property is activation of K+ uptake by an increase in medium osmolarity. This response is modulated by both internal and external concentrations of K+. Kdp is the only K(+)-transport system whose expression is regulated by environmental conditions. Decrease in turgor pressure and/or reduction in external K+ rapidly increase expression of Kdp. The signal created by these changes, inferred to be reduced turgor, is transmitted by the KdpD sensor kinase to the KdpE-response regulator that in turn stimulates transcription of the kdp genes. K+ acts as a cytoplasmic-signaling molecule, activating and/or inducing enzymes and transport systems that allow the cell to adapt to elevated osmolarity. The signal could be ionic strength or specifically K+. This signaling response is probably mediated by a direct sensing of internal ionic strength by each particular system and not by a component or system that coordinates this response by different systems to elevated K+.
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              Systematic identification of conserved bacterial c-di-AMP receptor proteins.

              R. M. Corrigan, I. Campeotto, T Jeganathan … (2013)
              Nucleotide signaling molecules are important messengers in key pathways that allow cellular responses to changing environments. Canonical secondary signaling molecules act through specific receptor proteins by direct binding to alter their activity. Cyclic diadenosine monophosphate (c-di-AMP) is an essential signaling molecule in bacteria that has only recently been discovered. Here we report on the identification of four Staphylococcus aureus c-di-AMP receptor proteins that are also widely distributed among other bacteria. Using an affinity pull-down assay we identified the potassium transporter-gating component KtrA as a c-di-AMP receptor protein, and it was further shown that this protein, together with c-di-AMP, enables S. aureus to grow in low potassium conditions. We defined the c-di-AMP binding activity within KtrA to the RCK_C (regulator of conductance of K(+)) domain. This domain is also found in a second S. aureus protein, a predicted cation/proton antiporter, CpaA, which as we show here also directly binds c-di-AMP. Because RCK_C domains are found in proteinaceous channels, transporters, and antiporters from all kingdoms of life, these findings have broad implications for the regulation of different pathways through nucleotide-dependent signaling. Using a genome-wide nucleotide protein interaction screen we further identified the histidine kinase protein KdpD that in many bacteria is also involved in the regulation of potassium transport and a PII-like signal transduction protein, which we renamed PstA, as c-di-AMP binding proteins. With the identification of these widely distributed c-di-AMP receptor proteins we link the c-di-AMP signaling network to a central metabolic process in bacteria.
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                Author and article information

                Journal
                Journal ID (nlm-ta): mBio
                Journal ID (iso-abbrev): MBio
                Journal ID (hwp): mbio
                Journal ID (pmc): mbio
                Journal ID (publisher-id): mBio
                Title: mBio
                Publisher: American Society of Microbiology (1752 N St., N.W., Washington, DC )
                ISSN (Electronic): 2150-7511
                Publication date (Electronic): 8 October 2013
                Publication date Collection: Sep-Oct 2013
                Volume: 4
                Issue: 5
                Electronic Location Identifier: e00784-13
                Affiliations
                [1]Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London, United Kingdom
                Author notes
                Address correspondence to a.grundling@ 123456imperial.ac.uk .
                Article
                Publisher ID: mBio00784-13
                DOI: 10.1128/mBio.00784-13
                PMC ID: 3791899
                PubMed ID: 24105767
                SO-VID: ee8c6d07-cd78-4339-92b6-9d4a6c93ef66
                Copyright © Copyright © 2013 Gründling.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution 3.0 Unported license.

                History
                Page count
                Pages: 3
                Categories
                Subject: Commentary
                Custom metadata
                cover-date September/October 2013

                ScienceOpen disciplines: Life sciences
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                ScienceOpen disciplines: Life sciences

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