Formation and transfer of disulphide bonds in living cells

This review focuses on the emerging similarities between the prokaryotic and eukaryotic systems that catalyse the formation of structural disulphide bonds, and the general principles of disulphide-bond formation that can be deduced from the genetic, biochemical and structural studies of these systems

Carolyn S. Sevier; Chris A. Kaiser

2002

Scholarcy highlights

  • Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and the periplasmic space of prokaryotic cells
  • This review focuses on the emerging similarities between the prokaryotic and eukaryotic systems that catalyse the formation of structural disulphide bonds, and the general principles of disulphide-bond formation that can be deduced from the genetic, biochemical and structural studies of these systems
  • The complete reconstitution of the Ero1–protein disulphide isomerase pathway for protein oxidation in vitro indicates that glutathione oxidation is driven by Ero1-derived disulphide bonds in PDI and/or substrate proteins
  • In the Erv pathway, the flavin cofactor of Erv interacts directly with molecular oxygen to contribute the oxidizing equivalents that are necessary for disulphide-bond formation
  • When the active sites are in a reduced form, PDI can catalyse the reduction of mispaired thiol residues, functioning as a disulphide reductase or isomerase
  • Cell Biol.152 553562.This study addresses the functional differences between yeast PDI and the four yeast PDI homologues, and illustrates some of the difficulties in sorting out the overlapping functions of the PDI homologues
  • A soluble protein with two thioredoxin-like domains that each contain a redox-active cysteine pair that donates disulphide bonds to newly synthesized proteins in the eukaryotic endoplasmic reticulum

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