ArticleThe Journal of biological chemistry2020
Protein secondary structure determines the temporal relationship between folding and disulfide formation.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Cancer Cell Line Classification Using Raman Spectroscopy of Cancer-Derived Exosomes and Machine Learning.Analytical chemistry · 2025Article
- Translation Rates and Protein Folding.Journal of molecular biology · 2024Review
- Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain.Biophysical journal · 2023Article
- Distinct role of ERp57 and ERdj5 as a disulfide isomerase and reductase during ER protein folding.Journal of cell science · 2023Article
- Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside.Frontiers in cell and developmental biology · 2023Review
- Calcium dysregulation potentiates wild-type myocilin misfolding: implications for glaucoma pathogenesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation.iScience · 2021Article
- Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.Nature communications · 2020Article
- Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway.Cells · 2020Review
- The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins.Journal of cell science · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
How and when disulfide bonds form in proteins relative to the stage of their folding is a fundamental question in cell biology. Two models describe this relationship: the folded precursor model, in which a nascent structure forms before disulfides do, and the quasi-stochastic model, where disulfides form prior to folding. Here we investigated oxidative folding of three structurally diverse substrates, β2-microglobulin, prolactin, and the disintegrin domain of ADAM metallopeptidase domain 10 (ADAM10), to understand how these mechanisms apply in a cellular context. We used a eukaryotic cell-free translation system in which we could identify disulfide isomers in stalled translation intermediates to characterize the timing of disulfide formation relative to translocation into the endoplasmic reticulum and the presence of non-native disulfides. Our results indicate that in a domain lacking secondary structure, disulfides form before conformational folding through a process prone to nonnative disulfide formation, whereas in proteins with defined secondary structure, native disulfide formation occurs after partial folding. These findings reveal that the nascent protein structure promotes correct disulfide formation during cotranslational folding.
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Registered trials
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