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- W4205264261 abstract "Proteins unfold constantly in cells, especially under stress conditions. Degradation of denatured polypeptides by Lon and related ATP-dependent AAA(+) proteases helps prevent toxic aggregates formation and other deleterious consequences, but how these destructive enzymatic machines distinguish between damaged and properly folded proteins is poorly understood. Here, we show that Escherichia coli Lon recognizes specific sequences -- rich in aromatic residues -- that are accessible in unfolded polypeptides but hidden in most native structures. Denatured polypeptides lacking such sequences are poor substrates. Lon also unfolds and degrades stably folded proteins with accessible recognition tags. Thus, protein architecture and the positioning of appropriate targeting sequences allow Lon degradation to be dependent or independent of the folding status of a protein. Our results suggest that Lon can recognize multiple signals in unfolded polypeptides synergistically, resulting in nanomolar binding and a mechanism for discriminating irreversibly damaged proteins from transiently unfolded elements of structure. PMID: 18708584 Funding information This work was supported by: NIAID NIH HHS, United States Grant ID: AI 16892 NIAID NIH HHS, United States Grant ID: R01 AI016892" @default.
- W4205264261 created "2022-01-25" @default.
- W4205264261 creator A5062563213 @default.
- W4205264261 date "2008-10-01" @default.
- W4205264261 modified "2023-10-16" @default.
- W4205264261 title "Faculty Opinions recommendation of Recognition of misfolded proteins by Lon, a AAA(+) protease." @default.
- W4205264261 doi "https://doi.org/10.3410/f.1123038.580150" @default.
- W4205264261 hasPublicationYear "2008" @default.
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