ArticleProceedings of the National Academy of Sciences of the United States of America2007
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
27 citing papers in PubMed, 56 citations in OpenAlex.
- Article
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dry molten globule conformational state of CYP11A1 (SCC) regulates the first step of steroidogenesis in the mitochondrial matrix.iScience · 2024Article
- Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.eLife · 2020Article
- Evolutionarily Related Dihydrofolate Reductases Perform Coequal Functions Yet Show Divergence in Their Trajectories.The protein journal · 2018Review
- Single-molecule nanopore enzymology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Coexistence of multiple minor states of fatty acid binding protein and their functional relevance.Scientific reports · 2016Article
- Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity.Frontiers in molecular biosciences · 2016Review
- Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.Molecular biology of the cell · 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
- Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates.The Journal of biological chemistry · 2014Article
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
- Chaperonin-mediated protein folding.The Journal of biological chemistry · 2013Article
- Effects of interactions with the GroEL cavity on protein folding rates.Biophysical journal · 2013Article
- Article
- Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR.FEBS letters · 2011Article
- Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.Journal of molecular biology · 2010Article
- Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density.Journal of biomolecular NMR · 2010Article
- Reconciling theories of chaperonin accelerated folding with experimental evidence.Cellular and molecular life sciences : CMLS · 2010Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
The chaperonin GroEL binds non-native polypeptides in an open ring via hydrophobic contacts and then, after ATP and GroES binding to the same ring as polypeptide, mediates productive folding in the now hydrophilic, encapsulated cis chamber. The nature of the folding reaction in the cis cavity remains poorly understood. In particular, it is unclear whether polypeptides take the same route to the native state in this cavity as they do when folding spontaneously free in solution. Here, we have addressed this question by using NMR measurements of the time course of acquisition of amide proton exchange protection of human dihydrofolate reductase (DHFR) during folding in the presence of methotrexate and ATP either free in solution or inside the stable cavity formed between a single ring variant of GroEL, SR1, and GroES. Recovery of DHFR refolded by the SR1/GroES-mediated reaction is 2-fold higher than in the spontaneous reaction. Nevertheless, DHFR folding was found to proceed by the same trajectories inside the cis folding chamber and free in solution. These observations are consistent with the description of the chaperonin chamber as an "Anfinsen cage" where polypeptide folding is determined solely by the amino acid sequence, as it is in solution. However, if misfolding occurs in the confinement of the chaperonin cavity, the polypeptide chain cannot undergo aggregation but rather finds its way back to a productive pathway in a manner that cannot be accomplished in solution, resulting in the observed high overall recovery.
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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.