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  • Journal article

  • The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

    • Authors : Knoke, Lisa R. (2023)

  • The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative 14 power and the DsbC/D system as its complement for isomerization of non-native disulfides. 15 While the standard redox potentials of those systems are known, the in vivo redox potential 16 imposed onto protein thiol disulfide pairs in the periplasm remains unknown. Here, we used 17 genetically encoded redox probes (roGFP2 ...
  • Journal article

  • The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

    • Authors : Knoke, Lisa R. (2023)

  • The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative 14 power and the DsbC/D system as its complement for isomerization of non-native disulfides. 15 While the standard redox potentials of those systems are known, the in vivo redox potential 16 imposed onto protein thiol disulfide pairs in the periplasm remains unknown. Here, we used 17 genetically encoded redox probes (roGFP2 ...
  • Journal article

  • Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation

    • Authors : Bageshwar, Umesh K. (2021)

  • The twin-arginine translocation (Tat) pathway transports folded proteins across energetic membranes. Numerous Tat substrates contain co-factors that are inserted before transport with the assistance of redox enzyme maturation proteins (REMPs), which bind to the signal peptide of precursor proteins. How signal peptides are transferred from a REMP to a binding site on the Tat receptor complex remains unknown. Since the signal peptide mediates both ...