Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast

Abstract Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR). The mechanisms of disulfide bond formation have mainly bee...

Full description

Bibliographic Details
Main Authors: Arianna Palma, Lukas A. Rettenbacher, Antti Moilanen, Mirva Saaranen, Christian Pacheco-Martinez, Brigitte Gasser, Lloyd Ruddock
Format: Article
Language:English
Published: Nature Portfolio 2023-08-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-023-41375-z