ArticleProceedings of the National Academy of Sciences of the United States of America2008
Setting the chaperonin timer: a two-stroke, two-speed, protein machine.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- Cryo-EM structures of GroEL:ESiScience · 2022Article
- Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.Protein expression and purification · 2018Article
- GroEL actively stimulates folding of the endogenous substrate protein PepQ.Nature communications · 2017Article
- Measurement ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2017Article
- Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.Biophysics and physicobiology · 2016Review
- Engineering a nanopore with co-chaperonin function.Science advances · 2015Article
- Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL.The Journal of biological chemistry · 2014Article
- The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein.The Journal of biological chemistry · 2014Article
- Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent.Scientific reports · 2014Article
- B-cell epitopes in GroEL of Francisella tularensis.PloS one · 2014Article
- 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
- Measuring how much work the chaperone GroEL can do.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Protein science : a publication of the Protein Society · 2011Article
- Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Reconciling theories of chaperonin accelerated folding with experimental evidence.Cellular and molecular life sciences : CMLS · 2010Review
- Use of thallium to identify monovalent cation binding sites in GroEL.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
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Authors and funding
3 authors.
Funding
Abstract
In a study of the timing mechanism of the chaperonin nanomachine we show that the hemicycle time (HCT) is determined by the mean residence time (MRT) of GroES on the cis ring of GroEL. In turn, this is governed by allosteric interactions within the trans ring of GroEL. Ligands that enhance the R (relaxed) state (residual ADP, the product of the previous hemicycle, and K(+)) extend the MRT and the HCT, whereas ligands that enhance the T (taut) state (unfolded substrate protein, SP) decrease the MRT and the HCT. In the absence of SP, the chaperonin machine idles in the resting state, but in the presence of SP it operates close to the speed limit, set by the rate of ATP hydrolysis by the cis ring. Thus, the conformational states of the trans ring largely control the speed of the complete chaperonin cycle.
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