A periplasmic reducing system protects single cysteine residues from oxidation
| Autor: | Katleen Denoncin, Joris Messens, Pierre Morsomme, Jean-François Collet, Khadija Wahni, Kate S. Carroll, Didier Vertommen, Matthieu Depuydt, Stephen E. Leonard |
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| Rok vydání: | 2009 |
| Předmět: |
Proteomics
Molecular Sequence Data Protein Disulfide-Isomerases Models Biological Sulfenic Acids Substrate Specificity chemistry.chemical_compound Catalytic Domain Escherichia coli Metallothionein Amino Acid Sequence Cysteine Disulfides Peptide sequence Cysteine metabolism chemistry.chemical_classification Multidisciplinary Escherichia coli Proteins Periplasmic space Amino acid chemistry Biochemistry Periplasm Thiol Sulfenic acid Periplasmic Proteins Oxidoreductases Oxidation-Reduction Protein Binding |
| Zdroj: | Science (New York, N.Y.). 326(5956) |
| ISSN: | 1095-9203 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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