Engineered pathways for correct disulfide bond oxidation.

doi:10.1089/ars.2010.3782

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Article

Engineered pathways for correct disulfide bond oxidation.

Antioxidants & redox signaling - 15 Jun 2011

Ren Guoping, Bardwell James C A

Abstract excerpt

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...

Topics

Disulfides
Drug Resistance, Bacterial
Escherichia coli
Escherichia coli Proteins
Heat-Shock Proteins
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Oxidation-Reduction
Periplasmic Proteins
Protein Conformation
Protein Disulfide-Isomerases
Protein Engineering
Protein Folding
Serine Endopeptidases
beta-Lactamases

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Identifiers

PMID: 21250836
DOI: 10.1089/ars.2010.3782
PMCID: PMC3096521

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