Article
The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
Molecular microbiology - 1 Jan 2008
Vertommen Didier, Depuydt Matthieu, Pan Jonathan, Leverrier Pauline, Knoops Laurent, Szikora Jean-Pierre, Messens Joris, Bardwell James C A, Collet Jean-Francois
Abstract excerpt
In Escherichia coli, DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by DsbB, which generates disulphides from quinone reduction. DsbA is not known to have any proofreading activity and can form incorrect disulphides in proteins with multiple cysteines. These incorrect disulphides are thought to be corrected by a protein disulphide isomerase, DsbC, which is kept in the reduced and active...
Topics
- Cysteine
- Disulfides
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- Mass Spectrometry
- Models, Molecular
- Oligonucleotide Array Sequence Analysis
- Oxidation-Reduction
- Periplasmic Proteins
- Phenotype
- Protein Disulfide-Isomerases