Mechanisms of Oxidative Protein Folding in the Bacterial Cell Envelope
- 15 October 2010
- journal article
- review article
- Published by Mary Ann Liebert Inc in Antioxidants and Redox Signaling
- Vol. 13 (8), 1231-1246
- https://doi.org/10.1089/ars.2010.3187
Abstract
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 correct pairs of cysteines are joined during the process of protein folding. However, a number of fundamental questions about these processes remain, especially about how they occur inside the cell. In addition, recent recognition of the increasing diversity among bacteria in the disulfide bond–forming capacity and in the systems for introducing disulfide bonds into proteins is raising new questions. We review here the marked progress in this field and discuss important questions that remain for future studies. Antioxid. Redox Signal. 13, 1231–1246.Keywords
This publication has 123 references indexed in Scilit:
- Inhibition of bacterial disulfide bond formation by the anticoagulant warfarinProceedings of the National Academy of Sciences of the United States of America, 2009
- Detecting Folding Intermediates of a Protein as It Passes through the Bacterial Translocation ChannelCell, 2009
- The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteinsNature Structural & Molecular Biology, 2009
- Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBThe EMBO Journal, 2009
- Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasmProceedings of the National Academy of Sciences of the United States of America, 2009
- NMR Solution Structure of the Integral Membrane Enzyme DsbB: Functional Insights into DsbB-Catalyzed Disulfide Bond FormationMolecular Cell, 2008
- Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formationProceedings of the National Academy of Sciences of the United States of America, 2008
- Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibilityThe EMBO Journal, 2007
- Laboratory evolution of one disulfide isomerase to resemble anotherProceedings of the National Academy of Sciences of the United States of America, 2007
- UCSF Chimera?A visualization system for exploratory research and analysisJournal of Computational Chemistry, 2004