MilliporeSigma
  • Home
  • Search Results
  • Systematic identification of conserved bacterial c-di-AMP receptor proteins.

Systematic identification of conserved bacterial c-di-AMP receptor proteins.

Proceedings of the National Academy of Sciences of the United States of America (2013-05-15)
Rebecca M Corrigan, Ivan Campeotto, Tharshika Jeganathan, Kevin G Roelofs, Vincent T Lee, Angelika Gründling
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Potassium chloride, puriss. p.a., reag. ISO, reag. Ph. Eur., 99.5-100.5%
Sigma-Aldrich
Potassium chloride, BioXtra, ≥99.0%
Sigma-Aldrich
Potassium chloride solution, 0.075 M, sterile-filtered, BioXtra, suitable for cell culture
Sigma-Aldrich
Potassium chloride, for molecular biology, ≥99.0%
Sigma-Aldrich
Potassium chloride, powder, BioReagent, suitable for cell culture, suitable for insect cell culture, ≥99.0%
Sigma-Aldrich
Potassium chloride, AnhydroBeads, −10 mesh, 99.99% trace metals basis
Sigma-Aldrich
Potassium chloride, AnhydroBeads, −10 mesh, 99.999% trace metals basis
Sigma-Aldrich
Potassium chloride, 99.999% trace metals basis
Sigma-Aldrich
Potassium chloride, ≥99.99% trace metals basis
Supelco
Potassium chloride solution, conductance standard B acc. to ISO 7888, 0.01 M KCl
Supelco
Potassium chloride solution, conductance standard A acc. to ISO 7888, 0.1 M KCl
Sigma-Aldrich
Potassium chloride solution, BioUltra, for molecular biology, ~1 M in H2O
Sigma-Aldrich
Potassium chloride, tested according to Ph. Eur.
Sigma-Aldrich
Potassium chloride, BioUltra, for molecular biology, ≥99.5% (AT)
Supelco
Potassium chloride solution, for Ag/AgCl electrodes, ~3 M KCl, saturated with silver chloride
Supelco
Potassium chloride solution, conductance standard C acc. to ISO 7888, 0.001 M KCl
Supelco
Potassium chloride solution, BioUltra, ~3 M in H2O
Supelco
ISA (ionic strength adjustment solution: 1 M KCl), 1 M KCl
Sigma-Aldrich
Potassium chloride, puriss., meets analytical specification of Ph. Eur., BP, USP, FCC, E508, 99-100.5% (AT), ≤0.0001% Al
Sigma-Aldrich
Potassium chloride, puriss. p.a., ≥99.5% (AT)
Sigma-Aldrich
Potassium chloride, ACS reagent, 99.0-100.5%
Sigma-Aldrich
Potassium chloride, ReagentPlus®, ≥99.0%