Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference44 articles.
1. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
2. Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics.
3. Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.
4. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.
5. ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.
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