A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation
2009; American Association for the Advancement of Science; Volume: 326; Issue: 5956 Linguagem: Inglês
10.1126/science.1179557
ISSN1095-9203
AutoresMatthieu Depuydt, Stephen E. Leonard, Didier Vertommen, Katleen Denoncin, Pierre Morsomme, Khadija Wahni, Joris Messens, Kate S. Carroll, Jean‐François Collet,
Tópico(s)Peptidase Inhibition and Analysis
ResumoPeriplasmic 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.
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