ArticleeLife2014
Super Spy variants implicate flexibility in chaperone action.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 57 citations in OpenAlex.
- Repair of oxidized methionine residues in the chaperone Spy maintains periplasmic proteostasis under chlorite stress in Escherichia coli.PLoS biology · 2025Article
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- A hydrophilic polyimidazolium antibiotic targeting the membranes of Gram-negative bacteria.The Journal of antimicrobial chemotherapy · 2023Article
- Why are G-quadruplexes good at preventing protein aggregation?RNA biology · 2023Article
- Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.Cell · 2022Article
- Insights into the client protein release mechanism of the ATP-independent chaperone Spy.Nature communications · 2022Article
- GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.Biomolecules · 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
- Mechanism of the small ATP-independent chaperone Spy is substrate specific.Nature communications · 2021Article
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.The Journal of biological chemistry · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Dissecting the Functional Contributions of the Intrinsically Disordered C-terminal Tail of Bacillus subtilis FtsZ.Journal of molecular biology · 2020Article
- Ligand-induced disorder-to-order transitions characterized by structural proteomics and molecular dynamics simulations.Journal of proteomics · 2020Article
- Identifying dynamic, partially occupied residues using anomalous scattering.Acta crystallographica. Section D, Structural biology · 2019Article
- Protein folding while chaperone bound is dependent on weak interactions.Nature communications · 2019Article
- COACH-D: improved protein-ligand binding sites prediction with refined ligand-binding poses through molecular docking.Nucleic acids research · 2018Article
- Electrostatic interactions are important for chaperone-client interaction in vivo.Microbiology (Reading, England) · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Experimental study of the role of disorder in protein function is challenging. It has been proposed that proteins utilize disordered regions in the adaptive recognition of their various binding partners. However apart from a few exceptions, defining the importance of disorder in promiscuous binding interactions has proven to be difficult. In this paper, we have utilized a genetic selection that links protein stability to antibiotic resistance to isolate variants of the newly discovered chaperone Spy that show an up to 7 fold improved chaperone activity against a variety of substrates. These "Super Spy" variants show tighter binding to client proteins and are generally more unstable than is wild type Spy and show increases in apparent flexibility. We establish a good relationship between the degree of their instability and the improvement they show in their chaperone activity. Our results provide evidence for the importance of disorder and flexibility in chaperone function. DOI: http://dx.doi.org/10.7554/eLife.01584.001.
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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.