ArticleThe EMBO journal2010
Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 39 citations in OpenAlex.
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- Protein chain collapse modulation and folding stimulation by GroEL-ES.Science advances · 2022Article
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.eLife · 2020Article
- Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.Journal of biochemistry · 2018Article
- Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.The Journal of biological chemistry · 2015Article
- How do chaperonins fold protein?Biophysics (Nagoya-shi, Japan) · 2015Review
- Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy.Biophysical journal · 2014Article
- Probing water density and dynamics in the chaperonin GroEL cavity.Journal of the American Chemical Society · 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
- GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Effects of interactions with the GroEL cavity on protein folding rates.Biophysical journal · 2013Article
- Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL.Journal of chemical biology · 2013Article
- 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
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The current mechanistic model of chaperonin-assisted protein folding assumes that the substrate protein in the cage, formed by GroEL central cavity capped with GroES, is isolated from outside and exists as a free polypeptide. However, using ATPase-deficient GroEL mutants that keep GroES bound, we found that, in the rate-limiting intermediate of a chaperonin reaction, the unfolded polypeptide in the cage partly protrudes through a narrow space near the GroEL/GroES interface. Then, the entire polypeptide is released either into the cage or to the outside medium. The former adopts a native structure very rapidly and the latter undergoes spontaneous folding. Partition of the in-cage folding and the escape varies among substrate proteins and is affected by hydrophobic interaction between the polypeptide and GroEL cavity wall. The ATPase-active GroEL with decreased in-cage folding produced less of a native model substrate protein in Escherichia coli cells. Thus, the polypeptide in the critical GroEL-GroES complex is neither free nor completely confined in the cage, but it is interacting with GroEL's apical region, partly protruding to outside.
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