A microbial sensor for discovering structural probes of protein misfolding and aggregation.

ABSTRACT: In all cell types, protein homeostasis, or "proteostasis," is maintained by sophisticated quality control networks that regulate protein synthesis, folding, trafficking, aggregation, disaggregation, and degradation. In one notable example, Escherichia coli employ a proteostasis system that determines whether substrates of the twin-arginine translocation (Tat) pathway are correctly folded and thus suitable for transport across the tightly sealed cytoplasmic membrane. Herein, we review growing evidence that the Tat translocase itself discriminates folded proteins from those that are misfolded and/or aggregated, preferentially exporting only the former. Genetic suppressors that inactivate this mechanism have recently been isolated and provide direct evidence for the participation of the Tat t

SUBMITTER: Waraho-Zhmayev D 

PROVIDER: S-EPMC3609123 | biostudies-literature | 2013 Mar-Apr

REPOSITORIES: biostudies-literature