ArticleNature communications2017
GroEL actively stimulates folding of the endogenous substrate protein PepQ.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- Mechanisms of Enhanced Low-Temperature Lignocellulose Degradation by an ARTP-InducedMicroorganisms · 2026Article
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices.Protein science : a publication of the Protein Society · 2025Article
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins.Communications biology · 2025Article
- Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states.Nature communications · 2025Article
- An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography.Cell stress & chaperones · 2024Article
- Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.Nature structural & molecular biology · 2024Article
- Article
- Structural basis of substrate progression through the bacterial chaperonin cycle.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.Communications biology · 2023Article
- Optimization of a Digital Mass Filter for the Isolation of Intact Protein Complexes in Stability Zone 1,1.Analytical chemistry · 2023Article
- A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Insights into the client protein release mechanism of the ATP-independent chaperone Spy.Nature communications · 2022Article
- Protein chain collapse modulation and folding stimulation by GroEL-ES.Science advances · 2022Article
- Allosteric differences dictate GroEL complementation of E. coli.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- Cryo-EM structures of GroEL:ESiScience · 2022Article
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6 authors.
Funding
Abstract
Many essential proteins cannot fold without help from chaperonins, like the GroELS system of Escherichia coli. How chaperonins accelerate protein folding remains controversial. Here we test key predictions of both passive and active models of GroELS-stimulated folding, using the endogenous E. coli metalloprotease PepQ. While GroELS increases the folding rate of PepQ by over 15-fold, we demonstrate that slow spontaneous folding of PepQ is not caused by aggregation. Fluorescence measurements suggest that, when folding inside the GroEL-GroES cavity, PepQ populates conformations not observed during spontaneous folding in free solution. Using cryo-electron microscopy, we show that the GroEL C-termini make physical contact with the PepQ folding intermediate and help retain it deep within the GroEL cavity, resulting in reduced compactness of the PepQ monomer. Our findings strongly support an active model of chaperonin-mediated protein folding, where partial unfolding of misfolded intermediates plays a key role.
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