Article
Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.
Journal of bacteriology - 1 Dec 2001
Rizzitello A E, Harper J R, Silhavy T J
Abstract excerpt
The periplasm of Escherichia coli contains many proteins proposed to have redundant functions in protein folding. Using depletion analysis, we directly demonstrated that null mutations in skp and surA, as well as in degP and surA, result in synthetic phenotypes, suggesting that Skp, SurA, and DegP are functionally redundant. The Deltaskp surA::kan combination has a bacteriostatic effect and leads to...
Topics
- Bacterial Outer Membrane Proteins
- Carrier Proteins
- DNA Transposable Elements
- DNA-Binding Proteins
- Escherichia coli
- Escherichia coli Proteins
- Molecular Chaperones
- Mutation
- Peptidylprolyl Isomerase
- Periplasm
- Phenotype
- Porins
- Receptors, Virus