Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine.

ABSTRACT: Many organisms can adapt to changes in the solute content of their surroundings (i.e., the osmolarity). Hyperosmotic shock causes water efflux and a concomitant reduction in cell volume, which is countered by the accumulation of osmolytes. This volume reduction increases the crowded nature of the cytoplasm, which is expected to affect protein stability. In contrast to traditional theory, which predicts that more crowded conditions can only increase protein stability, recent work shows that crowding can destabilize proteins through transient attractive interactions. Here, we quantify protein stability in living Escherichia coli cells before and after hyperosmotic shock in the presence and absence of the osmolyte, glycine betaine. The 7-kDa N-terminal src-homology 3 domain of Drosophila sign

SUBMITTER: Stadmiller SS 

PROVIDER: S-EPMC5985519 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature