Supplementary Materials

Supplementary Materials for:

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

Christopher F. Schuster, Lauren E. Bellows, Tommaso Tosi, Ivan Campeotto, Rebecca M. Corrigan, Paul Freemont, Angelika Gründling*

*Corresponding author. Email: a.grundling{at}imperial.ac.uk

This PDF file includes:

  • Materials and Methods
  • Fig. S1. Identification of SACOL2453 (OpuCA) as a potential c-di-AMP target protein using a genome-wide DRaCALA screen.
  • Fig. S2. DRaCALAs with cleared cell lysates derived from E. coli strains producing different CBS domain–containing S. aureus proteins.
  • Fig. S3. Oligomeric state of the S. aureus OpuCA CBS domain in the crystal structure and in solution.
  • Fig. S4. Structure-based sequence alignment of the S. aureus OpuCA CBS domain with other ligand-bound CBS domains.
  • Fig. S5. OpuCA protein amounts in wild-type S. aureus, mutant, and complementation strains.
  • Fig. S6. Confirmed and putative osmolyte uptake systems in S. aureus strains.
  • Table S1. Data collection and refinement statistics (molecular replacement).
  • Table S2. Bacterial strains used in this study.
  • Table S3. Primers used in this study.
  • References (6377)

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Technical Details

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Citation: C. F. Schuster, L. E. Bellows, T. Tosi, I. Campeotto, R. M. Corrigan, P. Freemont, A. Gründling, The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus. Sci. Signal. 9, ra81 (2016).

© 2016 American Association for the Advancement of Science