ArticleThe EMBO journal2008
Essential role of the chaperonin folding compartment in vivo.
Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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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Who cites it
38 citing papers in PubMed, 73 citations in OpenAlex.
- Virulence arsenal of Acinetobacter baumannii: mechanisms driving persistence and resistance.Archives of microbiology · 2026Review
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins.Communications biology · 2025Article
- A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.Journal of biochemistry · 2018Article
- From chaperonins to Rubisco assembly and metabolic repair.Protein science : a publication of the Protein Society · 2017Review
- GroEL actively stimulates folding of the endogenous substrate protein PepQ.Nature communications · 2017Article
- Dynamic unwrapping of nucleosomes by HsRAD51 that includes sliding and rotational motion of histone octamers.Nucleic acids research · 2017Article
- Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.Journal of bacteriology · 2016Article
- A Mutant Chaperonin That Is Functional at Lower Temperatures Enables Hyperthermophilic Archaea To Grow under Cold-Stress Conditions.Journal of bacteriology · 2015Article
- Multiple chaperonins in bacteria--novel functions and non-canonical behaviors.Cell stress & chaperones · 2015Review
- 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
- GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.Cell · 2014Article
- FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts.Chemistry & biology · 2013Article
- Role of nonspecific interactions in molecular chaperones through model-based bioinformatics.Biophysical journal · 2012Article
- Distinct features of protein folding by the GroEL system from a psychrophilic bacterium, Colwellia psychrerythraea 34H.Extremophiles : life under extreme conditions · 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
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The GroEL/GroES chaperonin system of Escherichia coli forms a nano-cage allowing single protein molecules to fold in isolation. However, as the chaperonin can also mediate folding independently of substrate encapsulation, it remained unclear whether the folding cage is essential in vivo. To address this question, we replaced wild-type GroEL with mutants of GroEL having either a reduced cage volume or altered charge properties of the cage wall. A stepwise reduction in cage size resulted in a gradual loss of cell viability, although the mutants bound non-native protein efficiently. Strikingly, a mild reduction in cage size increased the yield and the apparent rate of green fluorescent protein folding, consistent with the view that an effect of steric confinement can accelerate folding. As shown in vitro, the observed acceleration of folding was dependent on protein encapsulation by GroES but independent of GroES cycling regulated by the GroEL ATPase. Altering the net-negative charge of the GroEL cage wall also strongly affected chaperonin function. Based on these findings, the GroEL/GroES compartment is essential for protein folding in vivo.
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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.