Article
Identification of a protein required for disulfide bond formation in vivo.
Cell - 1 Nov 1991
Bardwell J C, McGovern K, Beckwith J
Abstract excerpt
We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells, pulse-labeled beta-lactamase, alkaline phosphatase, and OmpA are secreted but largely lack disulfide bonds. These disulfideless proteins may represent in vivo folding intermediates, since they are protease sensitive and chase slowly into stable oxidized forms. The dsbA gene codes for a...
Topics
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins
- Base Sequence
- Disulfides
- Escherichia coli
- Genes, Bacterial
- Genetic Complementation Test
- In Vitro Techniques
- Insulin
- Isomerases
- Molecular Sequence Data