Measurement of Protein Mobility in Reveals a Unique Tolerance to Osmotic Stress and Temperature Dependence of Diffusion.

Protein mobility in the cytoplasm is essential for cellular functions, and slow diffusion may limit the rates of biochemical reactions in the living cell. Here, we determined the apparent lateral diffusion coefficient ( ) of GFP in as a function of osmotic stress, temperature, and media composition. We find that is much less affected by hyperosmotic stress in than under similar conditions in and . We find a temperature optimum for protein diffusion in at 30°C, which deviates from predicted trends from the generalized Stokes-Einstein equation under dilute conditions and suggests that the structure of the cytoplasm and macromolecular crowding vary as a function of temperature. The turgor pressure of is comparable to other Gram-positive bacteria like and but higher in a knockout strain lacking the stress-inducible sigma factor SigB. We discuss these findings in the context of how survives during environmental transmission and interaction with the human host.