ArticleThe Journal of biological chemistry2013
Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress.Science advances · 2026Article
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones.Frontiers in molecular biosciences · 2022Article
- Article
- Temperature-Dependent Nanomechanics and Topography of Bacteriophage T7.Journal of virology · 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
- The chaperone toolbox at the single-molecule level: From clamping to confining.Protein science : a publication of the Protein Society · 2017Review
- GroEL actively stimulates folding of the endogenous substrate protein PepQ.Nature communications · 2017Article
- Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Scientific reports · 2015Article
- How do chaperonins fold protein?Biophysics (Nagoya-shi, Japan) · 2015Review
- 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
- Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
A key constraint on the growth of most organisms is the slow and inefficient folding of many essential proteins. To deal with this problem, several diverse families of protein folding machines, known collectively as molecular chaperones, developed early in evolutionary history. The functional role and operational steps of these remarkably complex nanomachines remain subjects of active debate. Here we present evidence that, for the GroEL-GroES chaperonin system, the non-native substrate protein enters the folding cycle on the trans ring of the double-ring GroEL-ATP-GroES complex rather than the ADP-bound complex. The properties of this ATP complex are designed to ensure that non-native substrate protein binds first, followed by ATP and finally GroES. This binding order ensures efficient occupancy of the open GroEL ring and allows for disruption of misfolded structures through two phases of multiaxis unfolding. In this model, repeated cycles of partial unfolding, followed by confinement within the GroEL-GroES chamber, provide the most effective overall mechanism for facilitating the folding of the most stringently dependent GroEL substrate proteins.
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