ArticleProceedings of the National Academy of Sciences of the United States of America1993
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 178 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins.International journal of molecular sciences · 2023Review
- The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis.Journal of molecular biology · 2015Review
- Chaperonin-mediated protein folding.The Journal of biological chemistry · 2013Article
- Chaperone-assisted protein folding: the path to discovery from a personal perspective.Nature medicine · 2011Article
- Protein folding in the cell: an inside story.Nature medicine · 2011Article
- Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Journal of amino acids · 2011Article
- GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?International journal of molecular sciences · 2009Review
- Biography of Arthur L. Horwich.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- A mobile loop order-disorder transition modulates the speed of chaperonin cycling.Protein science : a publication of the Protein Society · 2004Article
- Assembly of chaperonin complexes.Molecular biotechnology · 2001Review
- Single-particle selection and alignment with heavy atom cluster-antibody conjugates.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains.Protein science : a publication of the Protein Society · 1998Article
- The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphid.Journal of virology · 1997Article
- GroEL-mediated protein folding.Protein science : a publication of the Protein Society · 1997Review
- Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling.Protein science : a publication of the Protein Society · 1996Article
- Novel isolation method and structural stability of a eukaryotic chaperonin: the TCP-1 ring complex from rabbit reticulocytes.Protein science : a publication of the Protein Society · 1996Article
- Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.Protein science : a publication of the Protein Society · 1996Article
- Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 1996Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperonins are oligomeric protein complexes that play an essential role in the cell, mediating ATP-dependent polypeptide chain folding in a variety of cellular compartments. They appear to bind early folding intermediates, preventing their aggregation; in the presence of MgATP and a cochaperonin, bound polypeptides are released in a stepwise manner, associated with folding to the native state. Chaperonin complexes appear in the electron microscope as cylindrical structures, usually composed of two stacked rings, each containing, by negative staining, an electron dense central "hole" approximately 6.0 nm in diameter. We sought to identify the site on the Escherichia coli chaperonin groEL, where the "molten globule"-like intermediate of dihydrofolate reductase (DHFR) becomes bound, by examining in the scanning transmission electron microscope complexes formed between groEL and DHFR molecules bearing covalently crosslinked 1.4-nm gold clusters. In top views of the groEL complexes, gold densities were observed in the central region; in side views, the densities were seen at the end portions of the cylinders, corresponding to positions within the individual rings. In some cases, two gold densities were observed in the same groEL complex. We conclude that folding intermediates are bound inside central cavities within individual chaperonin rings. In this potentially sequestered location, folding intermediates with a compact conformation can be bound at multiple sites by surrounding monomeric members of the ring; localization of folding within the cavity could also facilitate rebinding of structures that initially fail to incorporate properly into the folding protein.
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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.