ArticleNature structural & molecular biology2011
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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Who cites it
104 citing papers in PubMed, 172 citations in OpenAlex.
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- Functional Characterization of the Histidine Kinase BaeS Reveals Critical Residues for BaeSR-Dependent Stress Signaling inMicroorganisms · 2026Article
- Structural basis of chaperone mechanisms in cells and the evolutionary emergence of the protein world.bioRxiv : the preprint server for biology · 2026Article
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- ThemBio · 2026Article
- Biophysical insights into recombinant Zeocin binding protein: conformational stability and folding dynamics across pH and temperature.Frontiers in molecular biosciences · 2026Article
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- Repair of oxidized methionine residues in the chaperone Spy maintains periplasmic proteostasis under chlorite stress in Escherichia coli.PLoS biology · 2025Article
- 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
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Mechanisms ofMicroorganisms · 2025Article
- Engineering a membrane protein chaperone to ameliorate the proteotoxicity of mutant huntingtin.Nature communications · 2025Article
- Global quantitative proteome analysis of a multi-resistantFrontiers in microbiology · 2025Article
- Making Proteins with Electricity.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Whole Cell Luminescence-Based Screen for Inhibitors of the Bacterial Sec Machinery.Biochemistry · 2024Article
- SAS: Split antibiotic selection for identifying chaperones that improve protein solubility.Heliyon · 2024Article
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- A hydrophilic polyimidazolium antibiotic targeting the membranes of Gram-negative bacteria.The Journal of antimicrobial chemotherapy · 2023Article
44 more citing papers are in PubMed but not listed here.
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
To optimize the in vivo folding of proteins, we linked protein stability to antibiotic resistance, thereby forcing bacteria to effectively fold and stabilize proteins. When we challenged Escherichia coli to stabilize a very unstable periplasmic protein, it massively overproduced a periplasmic protein called Spy, which increases the steady-state levels of a set of unstable protein mutants up to 700-fold. In vitro studies demonstrate that the Spy protein is an effective ATP-independent chaperone that suppresses protein aggregation and aids protein refolding. Our strategy opens up new routes for chaperone discovery and the custom tailoring of the in vivo folding environment. Spy forms thin, apparently flexible cradle-shaped dimers. The structure of Spy is unlike that of any previously solved chaperone, making it the prototypical member of a new class of small chaperones that facilitate protein refolding in the absence of energy cofactors.
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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.