ArticleProceedings of the National Academy of Sciences of the United States of America2010
Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study.The journal of physical chemistry letters · 2023Article
- Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.Nature chemical biology · 2018Article
- Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Tracking Equilibrium and Nonequilibrium Shifts in Data with TREND.Biophysical journal · 2017Article
- Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Biomolecular robotics for chemomechanically driven guest delivery fuelled by intracellular ATP.Nature chemistry · 2013Article
- Article
- Conformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulations.PLoS computational biology · 2011Article
- Single-molecule spectroscopy of protein folding in a chaperonin cage.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The molecular chaperone GroEL exists in at least two allosteric states, T and R, that interconvert in an ATP-controlled manner. Thermodynamic analysis suggests that the T-state population becomes negligible with increasing ATP concentrations, in conflict with the requirement for conformational cycling, which is essential for the operation of molecular machines. To solve this conundrum, we performed fluorescence correlation spectroscopy on the single-ring version of GroEL, using a fluorescent switch recently built into its structure, which turns "on," i.e., increases its fluorescence dramatically, when ATP is added. A series of correlation functions was measured as a function of ATP concentration and analyzed using singular-value decomposition. The analysis assigned the signal to two states whose dynamics clearly differ. Surprisingly, even at ATP saturation, approximately 50% of the molecules still populate the T state at any instance of time, indicating constant out-of-equilibrium cycling between T and R. Only upon addition of the cochaperonin GroES does the T-state population vanish. Our results suggest a model in which the T/R ratio is controlled by the rate of ADP release after hydrolysis, which can be determined accordingly.
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