ArticleThe Journal of biological chemistry2008
Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 48 citations in OpenAlex.
- From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study.The journal of physical chemistry letters · 2023Article
- Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.Scientific reports · 2021Article
- Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.International journal of molecular sciences · 2018Article
- A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.Frontiers in molecular biosciences · 2018Review
- Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis.Frontiers in molecular biosciences · 2017Review
- Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.Frontiers in molecular biosciences · 2016Review
- Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.Biophysics and physicobiology · 2016Review
- 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
- Crystal structure of the human mitochondrial chaperonin symmetrical football complex.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.Proceedings of the National Academy of Sciences of the United States of America · 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
- Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- ATP-driven molecular chaperone machines.Biopolymers · 2013Review
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
- Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.The Journal of biological chemistry · 2012Article
- Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside.The EMBO journal · 2010Article
- Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.The Journal of biological chemistry · 2010Article
- Reconciling theories of chaperonin accelerated folding with experimental evidence.Cellular and molecular life sciences : CMLS · 2010Review
- Probing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GroEL is an Escherichia coli chaperonin that is composed of two heptameric rings stacked back-to-back. GroEL assists protein folding with its cochaperonin GroES in an ATP-dependent manner in vitro and in vivo. However, it is still unclear whether GroES binds to both rings of GroEL simultaneously under physiological conditions. In this study, we monitored the GroEL-GroES interaction in the reaction cycle using fluorescence resonance energy transfer. We found that nearly equivalent amounts of symmetric GroEL-(GroES)(2) (football-shaped) complex and asymmetric GroEL-GroES (bullet-shaped) complex coexist during the functional reaction cycle. We also found that D398A, an ATP hydrolysis defective mutant of GroEL, forms a football-shaped complex with ATP bound to the two rings. Furthermore, we showed that ADP prevents the association of ATP to the trans-ring of GroEL, and as a consequence, the second GroES cannot bind to GroEL. Considering the concentrations of ADP and ATP in E. coli, ADP is expected to have a small effect on the inhibition of GroES binding to the trans-ring of GroEL in vivo. These results suggest that we should reconsider the chaperonin-mediated protein-folding mechanism that involves the football-shaped complex.
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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.