Catalysis of Oxidative Protein Folding by Mutants of Protein Disulfide Isomerase with a Single Active-Site Cysteine†

Biochemistry ◽  
1996 ◽  
Vol 35 (6) ◽  
pp. 1972-1980 ◽  
Author(s):  
Kenneth W. Walker ◽  
Michelle M. Lyles ◽  
Hiram F. Gilbert
Keyword(s):  
Protein Folding ◽  
Active Site ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Active Site Cysteine ◽  
Oxidative Protein Folding ◽  
Protein Disulfide

scholarly journals Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)–protein disulfide-isomerase relay when protein folding capacity is exceeded

2020 ◽  
Vol 295 (26) ◽  
pp. 8647-8655 ◽  
Author(s):  
Antti Moilanen ◽  
Lloyd W. Ruddock
Keyword(s):  
Protein Folding ◽  
Cross Talk ◽  
Protein Disulfide Isomerase ◽  
Feedback Inhibition ◽  
Inhibition Mechanism ◽  
Disulfide Isomerase ◽  
Unfolded Protein ◽  
Oxidative Protein Folding ◽  
Native Proteins ◽  
Protein Disulfide

Protein maturation in the endoplasmic reticulum (ER) depends on a fine balance between oxidative protein folding and quality control mechanisms, which together ensure high-capacity export of properly folded proteins from the ER. Oxidative protein folding needs to be regulated to avoid hyperoxidation. The folding capacity of the ER is regulated by the unfolded protein response (UPR) and ER-associated degradation (ERAD). The UPR is triggered by unfolded protein stress and leads to up-regulation of cellular components such as chaperones and folding catalysts. These components relieve stress by increasing folding capacity and up-regulating ERAD components that remove non-native proteins. Although oxidative protein folding and the UPR/ERAD pathways each are well-understood, very little is known about any direct cross-talk between them. In this study, we carried out comprehensive in vitro activity and binding assays, indicating that the oxidative protein folding relay formed by ER oxidoreductin 1 (Ero1), and protein disulfide-isomerase can be inactivated by a feedback inhibition mechanism involving unfolded proteins and folding intermediates when their levels exceed the folding capacity of the system. This mechanism allows client proteins to remain mainly in the reduced state and thereby minimizes potential futile oxidation–reduction cycles and may also enhance ERAD, which requires reduced protein substrates. Relief from excess levels of non-native proteins by increasing the levels of folding factors removed the feedback inhibition. These results reveal regulatory cross-talk between the oxidative protein folding and UPR and ERAD pathways.

Cigarette smoking affects oxidative protein folding in endoplasmic reticulum by modifying protein disulfide isomerase

2012 ◽  
Vol 27 (3) ◽  
pp. 965-977 ◽  
Author(s):  
Harshavardhan Kenche ◽  
Catherine J. Baty ◽  
Kokilavani Vedagiri ◽  
Steven D. Shapiro ◽  
Anna Blumental‐Perry
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Cigarette Smoking ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Oxidative Protein Folding ◽  
Protein Disulfide

scholarly journals The Contributions of Protein Disulfide Isomerase and Its Homologues to Oxidative Protein Folding in the Yeast Endoplasmic Reticulum

2004 ◽  
Vol 279 (48) ◽  
pp. 49780-49786 ◽  
Author(s):  
Ruoyu Xiao ◽  
Bonney Wilkinson ◽  
Anton Solovyov ◽  
Jakob R. Winther ◽  
Arne Holmgren ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Oxidative Protein Folding ◽  
Protein Disulfide

Bacterial protein disulfide isomerase: Efficient catalysis of oxidative protein folding at acidic pH

Biochemistry ◽  
1993 ◽  
Vol 32 (45) ◽  
pp. 12251-12256 ◽  
Author(s):  
Martina Wunderlich ◽  
Angelika Otto ◽  
Robert Seckler ◽  
Rudi Glockshuber
Keyword(s):  
Protein Folding ◽  
Protein Disulfide Isomerase ◽  
Acidic Ph ◽  
Bacterial Protein ◽  
Disulfide Isomerase ◽  
Oxidative Protein Folding ◽  
Protein Disulfide
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