ArticleChemical science2021
DsbA is a redox-switchable mechanical chaperone.
Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- An updated overview on the bacterial PhoP/PhoQ two-component signal transduction system.Frontiers in cellular and infection microbiology · 2025Review
- Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DsbA is a ubiquitous bacterial oxidoreductase that associates with substrates during and after translocation, yet its involvement in protein folding and translocation remains an open question. Here we demonstrate a redox-controlled chaperone activity of DsbA, on both cysteine-containing and cysteine-free substrates, using magnetic tweezers-based single molecule force spectroscopy that enables independent measurements of oxidoreductase activity and chaperone behavior. Interestingly we found that this chaperone activity is tuned by the oxidation state of DsbA; oxidized DsbA is a strong promoter of folding, but the effect is weakened by the reduction of the catalytic CXXC motif. We further localize the chaperone binding site of DsbA using a seven-residue peptide which effectively blocks the chaperone activity. We found that the DsbA assisted folding of proteins in the periplasm generates enough mechanical work to decrease the ATP consumption needed for periplasmic translocation by up to 33%.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.