Article
Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.
Science (New York, N.Y.) - 10 Dec 1993
Derman A I, Prinz W A, Belin D, Beckwith J
Abstract excerpt
Disulfide bonds are rarely found in cytoplasmic proteins. Mutations were selected for in Escherichia coli that allow disulfide bond formation in the cytoplasm. In the presence of these mutations, export-defective versions of alkaline phosphatase and mouse urokinase were able to fold into their en...
Topics
- Alkaline Phosphatase
- Cysteine
- Cytoplasm
- Disulfides
- Escherichia coli
- Genes, Bacterial
- Mutation
- Oxidation-Reduction
- Protein Folding
- Protein Sorting Signals
- Recombinant Proteins
- Thioredoxin-Disulfide Reductase
- Urokinase-Type Plasminogen Activator
