Engineered Pathways for Correct Disulfide Bond Oxidation
نویسندگان
چکیده
منابع مشابه
Engineered pathways for correct disulfide bond oxidation.
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 mut...
متن کاملEngineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.
In the Escherichia coli periplasm, the formation of protein disulfide bonds is catalyzed by DsbA and DsbC. DsbA is a monomer that is maintained in a fully oxidized state by the membrane enzyme DsbB, whereas DsbC is a dimer that is kept reduced by a second membrane protein, DsbD. Although the catalytic regions of DsbA and DsbC are composed of structurally homologous thioredoxin motif domains, Ds...
متن کاملElectron Avenue Pathways of Disulfide Bond Formation and Isomerization
extracytoplasmic environments (e.g., the lumen of the eukaryotic endoplasmic reticulum and the gram-negative bacterial periplasmic space). In contrast, the cytoplasm displays a network of enzymes and molecules dedicated to the reduction of disulfide bonds (Åslund Laurent Debarbieux and Jon Beckwith* Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 0...
متن کاملConservation and diversity of the cellular disulfide bond formation pathways.
Two pathways for the formation of biosynthetic protein disulfide bonds have been characterized in the endoplasmic reticulum (ER) of eukaryotes. In the major pathway, the membrane-associated flavoprotein Ero1 generates disulfide bonds for transfer to protein disulfide isomerase (PDI), which is responsible for directly introducing disulfide bonds into secretory proteins. In a minor fungal-specifi...
متن کاملA single disulfide bond differentiates aggregation pathways of beta2-microglobulin.
Deposition of wild-type beta2-microglobulin (beta2m) into amyloid fibrils is a complication in patients undergoing long-term hemodialysis. The native beta-sandwich fold of beta2m has a highly conserved disulfide bond linking Cys25 and Cys80. Oxidized beta2m forms needle-like amyloid fibrils at pH 2.5 in vitro, whereas reduced beta2m, at acid pH, in which the intra-chain disulfide bond is disrup...
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ژورنال
عنوان ژورنال: Antioxidants & Redox Signaling
سال: 2011
ISSN: 1523-0864,1557-7716
DOI: 10.1089/ars.2010.3782