ArticleNature structural & molecular biology2016
Substrate protein folds while it is bound to the ATP-independent chaperone Spy.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
53 citing papers in PubMed.
- A designed fusion tag improves soluble expression of nanobody inMagnetic resonance letters · 2026Article
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
- Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions.mSphere · 2025Article
- Making Proteins with Electricity.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.Nature communications · 2024Article
- A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.Molecular cell · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Trigger factor both holds and folds its client proteins.Nature communications · 2022Article
- Insights into the client protein release mechanism of the ATP-independent chaperone Spy.Nature communications · 2022Article
- Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding.International journal of molecular sciences · 2022Review
- The interactions of molecular chaperones with client proteins: why are they so weak?The Journal of biological chemistry · 2021Review
- Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.mBio · 2021Article
- A Conceptual Framework for Integrating Cellular Protein Folding, Misfolding and Aggregation.Life (Basel, Switzerland) · 2021Review
- Transcriptomic Analysis of the Activity and Mechanism of Action of a Ruthenium(II)-Based Antimicrobial That Induces Minimal Evolution of Pathogen Resistance.ACS pharmacology & translational science · 2021Article
- Mechanism of the small ATP-independent chaperone Spy is substrate specific.Nature communications · 2021Article
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Chaperones assist in the folding of many proteins in the cell. Although the most well-studied chaperones use cycles of ATP binding and hydrolysis to assist in protein folding, a number of chaperones have been identified that promote folding in the absence of high-energy cofactors. Precisely how ATP-independent chaperones accomplish this feat is unclear. Here we characterized the kinetic mechanism of substrate folding by the small ATP-independent chaperone Spy from Escherichia coli. Spy rapidly associates with its substrate, immunity protein 7 (Im7), thereby eliminating Im7's potential for aggregation. Remarkably, Spy then allows Im7 to fully fold into its native state while it remains bound to the surface of the chaperone. These results establish a potentially widespread mechanism whereby ATP-independent chaperones assist in protein refolding. They also provide compelling evidence that substrate proteins can fold while being continuously bound to a chaperone.
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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.