DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase. DsbG was also shown to interact with refolding intermediates of chemically denatured citrate synthase and p...

The human Anterior GRadient 2 (AGR2) protein is an Endoplasmic Reticulum (ER)-resident which belongs to the Protein-Disulfide Isomerase (PDI) superfamily and involved productive folding in ER. As such AGR2, often found overexpressed adenocarcinomas, contributes tumour development by enhancing ER proteostasis. We previously demonstrated that AGR2 secreted (extracellular (eAGR2)) microenvironment...

The ER (endoplasmic reticulum) has long been considered the plant cell compartment within which protein disulfide bond formation occurs. Members of the ER-located PDI (protein disulfide isomerase) family are responsible for oxidizing, reducing and isomerizing disulfide bonds, as well as functioning as chaperones to newly synthesized proteins. In the present study we demonstrate that an abundant...