Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals

Yoshimi Sato, Kenji Inaba

Research output: Contribution to journalShort surveypeer-review

62 Citations (Scopus)


Almost all organisms, from bacteria to humans, possess catalytic systems that promote disulfide bond formation-coupled protein folding, i.e. oxidative protein folding. These systems are necessary for the biosynthesis of many secretory and membrane proteins, such as antibodies, major histocompatibility complex molecules, growth factors, and insulin. Over the last decade, structural studies have made striking progress in this field of research, identifying how oxidative systems operate in a specific and regulated manner to maintain redox and protein homeostasis within cells. Interestingly, more and more novel catalysts that promote disulfide bond formation have been discovered in mammals, suggesting that the oxidative protein folding network is even more complicated in higher eukaryotes than previously thought. This review highlights the physiological roles and molecular bases of the disulfide bond formation pathways that have evolved in the bacterial periplasm and the endoplasmic reticulum of fungi and mammals. Accumulating knowledge about disulfide bond formation networks widely distributed throughout the biological kingdom has significantly advanced our understanding of the cellular mechanisms dedicated to protein quality control.

Original languageEnglish
Pages (from-to)2262-2271
Number of pages10
JournalFEBS Journal
Issue number13
Publication statusPublished - 2012 Jul 1
Externally publishedYes


  • Disulfide bond
  • DsbA
  • DsbB
  • Ero1
  • PDI
  • Prx4

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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