Ontology highlight
ABSTRACT:
SUBMITTER: Kadokura H
PROVIDER: S-EPMC2959184 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Kadokura Hiroshi H Beckwith Jon J
Antioxidants & redox signaling 20101001 8
Disulfide-bond formation is important for the correct folding of a great number of proteins that are exported to the cell envelope of bacteria. Bacterial cells have evolved elaborate systems to promote the joining of two cysteines to form a disulfide bond and to repair misoxidized proteins. In the past two decades, significant advances have occurred in our understanding of the enzyme systems (DsbA, DsbB, DsbC, DsbG, and DsbD) used by the gram-negative bacterium Escherichia coli to ensure that co ...[more]