The endoplasmic reticulum (ER) provides an environment that is highly optimized for
oxidative protein folding. Rather than relying on small molecule oxidants like glutathione, it …

Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

Bacillus subtilis is a rod-shaped, Gram-positive soil bacterium that secretes numerous
enzymes to degrade a variety of substrates, enabling the bacterium to survive in a …

Bacteria are simple and cost effective hosts for producing recombinant proteins. However,
their physiological features may limit their use for obtaining in native form proteins of some …

Envelope biogenesis and homeostasis in gram-negative bacteria are exceptionally intricate
processes that require a multitude of periplasmic chaperones to ensure cellular survival …

The endoplasmic reticulum (ER) supports disulfide formation through an essential protein
relay involving Ero1p and protein disulfide isomerase (PDI). We find that in addition to …

We describe a conserved yeast gene, ERO1, that is induced by the unfolded protein
response and encodes a novel glycoprotein required for oxidative protein folding in the ER …

Interest in protein disulfide bond formation has recently increased because of the prominent
role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that …

▪ Abstract Disulfide bonds formed between pairs of cysteines are important features of the
structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia …

The endoplasmic reticulum (ER) supports disulfide bond formation by a poorly understood
mechanism requiring protein disulfide isomerase (PDI) and ERO1. In yeast, Ero1p-mediated …