A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation
- 20 November 2009
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 326 (5956) , 1109-1111
Abstract
Periplasmic Redox Regulation: The oxidation state of intracellular and extracellular proteins are carefully managed by cellular redox machineries. Depuydt et al. (p. 1109 ) discovered a reducing system that protects single cysteine residues from oxidation in the bacterial periplasm. DsbG, a thioredoxin-related protein, appears to be a key player in that system and is the first reductase identified in the periplasm of Escherichia coli . Together with DsbC, DsbG controls the global sulfenic acid content of this compartment. Sulfenic acid formation is a major posttranslational modification in the periplasm, and three homologous L,D-transpeptidases are substrates of DsbG. Sulfenic acid formation is not restricted to E. coli , but is ubiquitous. Because proteins from the thioredoxin superfamily are widespread, similar thioredoxin-related proteins may control cellular sulfenic acid more widely.Keywords
This publication has 19 references indexed in Scilit:
- Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasmProceedings of the National Academy of Sciences, 2009
- Expanding the functional diversity of proteins through cysteine oxidationCurrent Opinion in Chemical Biology, 2008
- Unexpected Inhibition of Peptidoglycan LD-Transpeptidase from Enterococcus faecium by the β-Lactam ImipenemJournal of Biological Chemistry, 2007
- Identification of the l , d -Transpeptidases Responsible for Attachment of the Braun Lipoprotein to Escherichia coli PeptidoglycanJournal of Bacteriology, 2007
- Pathways of disulfide bond formation in Escherichia coliThe International Journal of Biochemistry & Cell Biology, 2006
- Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfideProceedings of the National Academy of Sciences, 2004
- How Thioredoxin can Reduce a Buried Disulphide BondJournal of Molecular Biology, 2004
- Thioredoxin links redox to the regulation of fundamental processes of plant mitochondriaProceedings of the National Academy of Sciences, 2004
- Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative FoldingScience, 2004
- Alkyl Hydroperoxide Reductase Is the Primary Scavenger of Endogenous Hydrogen Peroxide in Escherichia coliJournal of Bacteriology, 2001