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• W2048610367 startingPage "2399" @default.
• W2048610367 abstract "Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation. By linking correct disulfide bond formation to antibiotic resistance, we selected mutants that catalyze correct disulfide formation in the absence of DsbC, Escherichia coli's PDI. Most of our mutants massively overproduce the disulfide oxidase DsbA and change its redox status. They enhance DsbA's ability to directly form the correct disulfides by increasing the level of mixed disulfides between DsbA and substrate proteins. One mutant operates via a different mechanism; it contains mutations in DsbB and CpxR that alter the redox environment of the periplasm and increases the level of the chaperone/protease DegP, allowing DsbA to gain disulfide isomerase ability in vivo. Thus, given the proper expression level, redox status, and chaperone assistance, the oxidase DsbA can readily function in vivo to catalyze the folding of proteins with complex disulfide bond connectivities. Our selection reveals versatile strategies for correct disulfide formation in vivo. Remarkably, our evolution of new pathways for correct disulfide bond formation in E. coli mimics eukaryotic PDI, a highly abundant partially reduced protein with chaperone activity. Antioxid. Redox Signal. 14, 2399–2412." @default.
• W2048610367 created "2016-06-24" @default.
• W2048610367 creator A5012242924 @default.
• W2048610367 creator A5028008163 @default.
• W2048610367 date "2011-06-15" @default.
• W2048610367 modified "2023-10-16" @default.
• W2048610367 title "Engineered Pathways for Correct Disulfide Bond Oxidation" @default.
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• W2048610367 doi "https://doi.org/10.1089/ars.2010.3782" @default.
• W2048610367 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3096521" @default.
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