Article
Synthetic competition between cytoplasmic folding and translocation of a soluble membrane protein domain.
Research in microbiology - 1 Feb 1995
Uhland K, Zander T, Ehrmann M
Abstract excerpt
In wild-type strains of Escherichia coli, alkaline phosphatase (AP), either when present as a soluble protein or when fused to a membrane protein, is only active after translocation to the periplasm. In thioredoxin reductase (trxB) mutants, however, cytoplasmically localized AP can form disulphide bonds and can reach an active conformation. Once it has folded in the cytoplasm, it can no longer be translocated. On...
Topics
- Alkaline Phosphatase
- Bacterial Outer Membrane Proteins
- Cytoplasm
- Enzyme Activation
- Escherichia coli
- In Vitro Techniques
- Mutation