ArticleJournal of molecular biology2008
Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Unpicking allosteric mechanisms of homo-oligomeric proteins by determining their successive ligand binding constants.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.Journal of bacteriology · 2016Article
- Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis.Biophysical journal · 2012Article
- The GroEL/GroES cis cavity as a passive anti-aggregation device.FEBS letters · 2009Review
- Common crowding agents have only a small effect on protein-protein interactions.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The chaperonin GroEL assists protein folding by undergoing ATP-induced conformational changes that are concerted within each of its two back-to-back stacked rings. Here we examined whether concerted allosteric switching gives rise to all-or-none release and folding of domains in a chimeric fluorescent protein substrate, CyPet-YPet. Using this substrate, it was possible to determine the folding yield of each domain from its intrinsic fluorescence and that of the entire chimera by measuring Förster resonance energy transfer between the two domains. Hence, it was possible to determine whether release of one domain is accompanied by release of the other domain (concerted mechanism), or whether their release is not coupled. Our results show that the chimera's release tends to be concerted when folding is assisted by a wild-type GroEL variant, but not when assisted by the F44W/D155A mutant that undergoes a sequential allosteric switch. A connection between the allosteric mechanism of this molecular machine and its biological function in assisting folding is thus established.
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