Protein Folding Stability Changes Across the Proteome Reveal Targets of Cu Toxicity in E. coli.

ABSTRACT: The ability of metal ionophores to induce cellular metal hyperaccumulation endows them with potent antimicrobial activity; however, the targets and mechanisms behind these outcomes are not well understood. This work describes the first utilization of proteome-wide measurements of protein folding stability in combination with protein expression level analysis to identify protein targets of copper, thereby providing new insight into ionophore-induced copper toxicity in E. coli. The protein folding stability analysis employed a one-pot protocol for pulse proteolysis (PP) in combination with a semi-tryptic peptide enrichment strategy for proteolysis procedures (STEPP) to generate stability profiles for proteins in cell lysates derived fro

SUBMITTER: Wiebelhaus N 

PROVIDER: S-EPMC7984275 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature