ArticleThe Journal of biological chemistry2015
Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024Article
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- DsbA is a redox-switchable mechanical chaperone.Chemical science · 2021Article
- Protein folding modulates the chemical reactivity of a Gram-positive adhesin.Nature chemistry · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- The Mechanical Power of Titin Folding.Cell reports · 2019Article
- Mechanical architecture and folding of E. coli type 1 pilus domains.Nature communications · 2018Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins.Nature structural & molecular biology · 2017Article
- Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI).Scientific reports · 2017Article
- Tailoring protein nanomechanics with chemical reactivity.Nature communications · 2017Article
- Mechanical forces regulate the reactivity of a thioester bond in a bacterial adhesin.The Journal of biological chemistry · 2017Article
- Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.Nature communications · 2016Article
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Oxidative folding, the process by which proteins fold and acquire disulfide bonds concurrently, is of critical importance for a wide range of biological processes. Generally, this process is catalyzed by oxidoreductase enzymes that facilitate oxidation and also bear chaperone functionality. Although this process has been well described qualitatively, fine yet important details remain obscured by a limited quantitative perspective, arising from the limitations in the application of bulk biochemical methods to the study of oxidative folding. In this work, we have applied single molecule force spectroscopy techniques to monitor in real time the process of oxidative folding as catalyzed by DsbA, the enzyme solely responsible for the catalysis of oxidative folding in the bacterial periplasm. We provide a quantitative and detailed description of the catalytic mechanism utilized by DsbA that offers insight into the entire sequence of events that occurs in the periplasm from the unfolded-reduced state to the folded-oxidized protein. We have compared our results with those of protein disulfide-isomerase, the eukaryotic counterpart of DsbA, allowing us to devise a general mechanism for oxidative folding that also reflects upon the physiological functions and demands of these enzymes in vivo.
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