ArticleThe Journal of biological chemistry2020
Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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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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.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- A drug-microbiome-drug interaction impacts co-prescribed medications for Parkinson's disease.Nature microbiology · 2026Article
- Article
- Repair of oxidized methionine residues in the chaperone Spy maintains periplasmic proteostasis under chlorite stress in Escherichia coli.PLoS biology · 2025Article
- Making Proteins with Electricity.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Ionic Liquid-Based Strategy for Predicting Protein Aggregation Propensity and Thermodynamic Stability.JACS Au · 2022Article
- Insights into the client protein release mechanism of the ATP-independent chaperone Spy.Nature communications · 2022Article
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperones are essential components of the protein homeostasis network. There is a growing interest in optimizing chaperone function, but exactly how to achieve this aim is unclear. Here, using a model chaperone, the bacterial protein Spy, we demonstrate that substitutions that alter the electrostatic potential of Spy's concave, client-binding surface enhance Spy's anti-aggregation activity. We show that this strategy is more efficient than one that enhances the hydrophobicity of Spy's surface. Our findings thus challenge the traditional notion that hydrophobic interactions are the major driving forces that guide chaperone-substrate binding. Kinetic data revealed that both charge- and hydrophobicity-enhanced Spy variants release clients more slowly, resulting in a greater "holdase" activity. However, increasing short-range hydrophobic interactions deleteriously affected Spy's ability to capture substrates, thus reducing its
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Registered trials
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