ArticleProceedings of the National Academy of Sciences of the United States of America2010
Protein refolding by pH-triggered chaperone binding and release.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed, 1 synthesis or guideline pooled it, 93 citations in OpenAlex.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Acid-tolerant bacteria and prospects in industrial and environmental applications.Applied microbiology and biotechnology · 2023Review
- The pH Robustness of Bacterial Sensing.mBio · 2022Article
- Microreactor equipped with naturally acid-resistant histidine ammonia lyase from an extremophile.Materials advances · 2022Article
- Removal of disulfide from acid stress chaperone HdeA does not wholly eliminate structure or function at low pH.Biochemistry and biophysics reports · 2021Article
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
- Comparative Proteomic Analysis ofFrontiers in microbiology · 2021Article
- A metabolite binding protein moonlights as a bile-responsive chaperone.The EMBO journal · 2020Article
- Microbial response to acid stress: mechanisms and applications.Applied microbiology and biotechnology · 2020Review
- Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone.The Journal of biological chemistry · 2019Article
- Acid-denatured small heat shock protein HdeA fromThe Journal of biological chemistry · 2019Article
- In vivo chloride concentrations surge to proteotoxic levels during acid stress.Nature chemical biology · 2018Article
- The Mechanism of HdeA Unfolding and Chaperone Activation.Journal of molecular biology · 2018Article
- The Glutaminase-Dependent Acid Resistance System: Qualitative and Quantitative Assays and Analysis of Its Distribution in Enteric Bacteria.Frontiers in microbiology · 2018Article
- Stress-Activated Chaperones: A First Line of Defense.Trends in biochemical sciences · 2017Review
- Genetically encoded releasable photo-cross-linking strategies for studying protein-protein interactions in living cells.Nature protocols · 2017Article
- The Pentablock Amphiphilic Copolymer T1107 Prevents Aggregation of Denatured and Reduced Lysozyme.Macromolecular bioscience · 2017Article
- Article
- Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo.Journal of visualized experiments : JoVE · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Molecular chaperones are typically either adenosine triphosphate (ATP) dependent or rely heavily on their ATP-dependent chaperone counterparts in order to promote protein folding. This presents a challenge to chaperones that are localized to ATP-deficient cellular compartments. Here we describe a mechanism by which the pH-regulated acid stress chaperone HdeA is capable of independently facilitating the refolding of acid-denatured proteins in the bacterial periplasm, which lacks both ATP and ATP-dependent chaperone machines. Our results are consistent with a model in which HdeA stably binds substrates at low pH, thereby preventing their irreversible aggregation. pH neutralization subsequently triggers the slow release of substrate proteins from HdeA, keeping the concentration of aggregation-sensitive intermediates below the threshold where they begin to aggregate. This provides a straightforward and ATP-independent mechanism that allows HdeA to facilitate protein refolding. Unlike previously characterized chaperones, HdeA appears to facilitate protein folding by using a single substrate binding-release cycle. This cycle is entirely regulated by the external environment and is therefore energy-neutral for the bacteria.
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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.