ArticlePlant physiology2016
Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and 1 in Soybean.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions.Nature communications · 2023Article
- Endoplasmic reticulum oxidoreductin provides resilience against reductive stress and hypoxic conditions by mediating luminal redox dynamics.The Plant cell · 2022Article
- Metabolic Pathway of Natural Antioxidants, Antioxidant Enzymes and ROS Providence.Antioxidants (Basel, Switzerland) · 2022Review
- Expression Characterization ofInternational journal of molecular sciences · 2022Article
- Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding.Plant physiology · 2022Article
- Article
- CaMolecules (Basel, Switzerland) · 2021Article
- Conjugate of Thiol and Guanidyl Units with Oligoethylene Glycol Linkage for Manipulation of Oxidative Protein Folding.Molecules (Basel, Switzerland) · 2021Article
- Article
- PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.Molecules (Basel, Switzerland) · 2020Review
- Regulation of plant ER oxidoreductin 1 (ERO1) activity for efficient oxidative protein folding.The Journal of biological chemistry · 2019Article
- AtERO1 and AtERO2 Exhibit Differences in Catalyzing Oxidative Protein Folding in the Endoplasmic Reticulum.Plant physiology · 2019Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most proteins produced in the endoplasmic reticulum (ER) of eukaryotic cells fold via disulfide formation (oxidative folding). Oxidative folding is catalyzed by protein disulfide isomerase (PDI) and PDI-related ER protein thiol disulfide oxidoreductases (ER oxidoreductases). In yeast and mammals, ER oxidoreductin-1s (Ero1s) supply oxidizing equivalent to the active centers of PDI. In this study, we expressed recombinant soybean Ero1 (GmERO1a) and found that GmERO1a oxidized multiple soybean ER oxidoreductases, in contrast to mammalian Ero1s having a high specificity for PDI. One of these ER oxidoreductases, GmPDIM, associated in vivo and in vitro with GmPDIL-2, was unable to be oxidized by GmERO1a. We therefore pursued the possible cooperative oxidative folding by GmPDIM, GmERO1a, and GmPDIL-2 in vitro and found that GmPDIL-2 synergistically accelerated oxidative refolding. In this process, GmERO1a preferentially oxidized the active center in the A': domain among the A: , A': , and B: domains of GmPDIM. A disulfide bond introduced into the active center of the A': domain of GmPDIM was shown to be transferred to the active center of the A: domain of GmPDIM and the A: domain of GmPDIM directly oxidized the active centers of both the A: or A': domain of GmPDIL-2. Therefore, we propose that the relay of an oxidizing equivalent from one ER oxidoreductase to another may play an essential role in cooperative oxidative folding by multiple ER oxidoreductases in plants.
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