ArticleProceedings of the National Academy of Sciences of the United States of America2007
Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- Folding and assembly defects of pyruvate dehydrogenase deficiency-related variants in the E1α subunit of the pyruvate dehydrogenase complex.Cellular and molecular life sciences : CMLS · 2018Article
- Article
- 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
- Bacterial expression strategies for several Sus scrofa diacylglycerol kinase alpha constructs: solubility challenges.Scientific reports · 2013Article
- Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis.Biophysical journal · 2012Article
- Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization.Journal of bacteriology · 2009Article
- The GroEL/GroES cis cavity as a passive anti-aggregation device.FEBS letters · 2009Review
- Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET.Journal of molecular biology · 2008Article
- Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The double-ring chaperonin GroEL mediates protein folding, in conjunction with its helper protein GroES, by undergoing ATP-induced conformational changes that are concerted within each heptameric ring. Here we have examined whether the concerted nature of these transitions is responsible for protein substrate release in an all-or-none manner. Two chimeric substrates were designed, each with two different reporter activities that were recovered after denaturation in GroES-dependent and independent fashions, respectively. The refolding of the chimeras was monitored in the presence of GroEL variants that undergo ATP-induced intraring conformational changes that are either sequential (F44W/D155A) or concerted (F44W). Our results show that release of a protein substrate from GroEL in a domain-by-domain fashion is favored when the intraring allosteric transitions of GroEL are sequential and not concerted.
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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.