ArticleProceedings of the National Academy of Sciences of the United States of America2013
Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- In situ characterization of mitochondrial Hsp60-Hsp10 chaperone complex under folding stress.Science advances · 2025Article
- Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins.Communications biology · 2025Article
- Membrane-associated σ factors disrupt rRNA operon clustering in Escherichia coli.PLoS biology · 2025Article
- Low-temperature features of the psychrophilic chaperonin from Pseudoalteromonas haloplanktis.Archives of microbiology · 2024Article
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- Visualization of Sparsely-populated Lower-order Oligomeric States of Human Mitochondrial Hsp60 by Cryo-electron Microscopy.Journal of molecular biology · 2021Article
- Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.Scientific reports · 2021Article
- Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity.The journal of physical chemistry letters · 2021Article
- Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.Scientific reports · 2021Article
- Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL.Biochemistry · 2021Article
- OsCpn60β1 is Essential for Chloroplast Development in Rice (International journal of molecular sciences · 2020Article
- Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin.Nature communications · 2020Article
- Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020Review
- Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes.The Journal of biological chemistry · 2019Article
- The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed atomic force microscopy imaging.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.International journal of molecular sciences · 2018Article
- Folding of maltose binding protein outside of and in GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development.PLoS genetics · 2017Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using calibrated FRET, we show that the simultaneous occupancy of both rings of GroEL by ATP and GroES occurs, leading to the rapid formation of symmetric GroEL:GroES2 "football" particles regardless of the presence or absence of substrate protein (SP). In the absence of SP, these symmetric particles revert to asymmetric GroEL:GroES1 "bullet" particles. The breakage of GroES symmetry requires the stochastic hydrolysis of ATP and the breakage of nucleotide symmetry. These asymmetric particles are both persistent and dynamic; they turnover via the asymmetric cycle. When challenged with SP, however, they revert to symmetric particles within a second. In the presence of SP, the symmetric particles are also persistent and dynamic. They turn over via the symmetric cycle. Under these conditions, the stochastic hydrolysis of ATP and the breakage of nucleotide symmetry also occur within the ensemble of particles. However, on account of SP-catalyzed ADP/ATP exchange, GroES symmetry is rapidly restored. The residence time of both GroES and SP on functional GroEL is reduced to ∼1 s, enabling many more iterations than was previously believed possible, consistent with the iterative annealing mechanism. This result is inconsistent with currently accepted models. Using a foldable SP, we show that as the SP folds to the native state and the population of unfolded SP declines, the population of symmetric particles reverts to asymmetric particles in parallel, a result that is consistent with the former being the folding functional form.
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