1932

Abstract

It is now well established that protein folding requires the assistance of folding helpers in vivo. The formation or isomerization of disulfide bonds in proteins is a slow process requiring catalysis. In nascent polypeptide chains the cysteine residues are in the thiol form. The formation of the disulfide bonds usually occurs simultaneously with the folding of the polypeptide, which means in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. In prokaryotes, the existence of redox proteins involved in the formation of disulfide bonds containing proteins has recently been revealed in the periplasm. The discovery of these redox proteins through various genetic approaches will be summarized, as well as the most recent insights regarding their biochemical and biological activities.

Loading

Article metrics loading...

/content/journals/10.1146/annurev.micro.51.1.179
1997-10-01
2024-03-28
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.micro.51.1.179
Loading
/content/journals/10.1146/annurev.micro.51.1.179
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error