ArticleThe Journal of biological chemistry2008
Triggering protein folding within the GroEL-GroES complex.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- Article
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.Nature structural & molecular biology · 2024Article
- Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time.ACS central science · 2023Article
- Development and application of multicolor burst analysis spectroscopy.Biophysical journal · 2021Article
- GroEL Mediates Folding ofIndian journal of microbiology · 2018Article
- Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.Journal of biochemistry · 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
- 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
- Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.Biophysics and physicobiology · 2016Review
- 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
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
- Clathrin coat disassembly by the yeast Hsc70/Ssa1p and auxilin/Swa2p proteins observed by single-particle burst analysis spectroscopy.The Journal of biological chemistry · 2013Article
- Article
- Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.The Journal of biological chemistry · 2012Article
- Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The folding of many proteins depends on the assistance of chaperonins like GroEL and GroES and involves the enclosure of substrate proteins inside an internal cavity that is formed when GroES binds to GroEL in the presence of ATP. Precisely how assembly of the GroEL-GroES complex leads to substrate protein encapsulation and folding remains poorly understood. Here we use a chemically modified mutant of GroEL (EL43Py) to uncouple substrate protein encapsulation from release and folding. Although EL43Py correctly initiates a substrate protein encapsulation reaction, this mutant stalls in an intermediate allosteric state of the GroEL ring, which is essential for both GroES binding and the forced unfolding of the substrate protein. This intermediate conformation of the GroEL ring possesses simultaneously high affinity for both GroES and non-native substrate protein, thus preventing escape of the substrate protein while GroES binding and substrate protein compaction takes place. Strikingly, assembly of the folding-active GroEL-GroES complex appears to involve a strategic delay in ATP hydrolysis that is coupled to disassembly of the old, ADP-bound GroEL-GroES complex on the opposite ring.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.