ArticleThe Journal of biological chemistry2012
Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- Genomic and phenotypic characterization of a red-pigmented strain ofFrontiers in microbiology · 2023Article
- Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020Review
- Signalling networks and dynamics of allosteric transitions in bacterial chaperonin GroEL: implications for iterative annealing of misfolded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed atomic force microscopy imaging.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- The chaperone toolbox at the single-molecule level: From clamping to confining.Protein science : a publication of the Protein Society · 2017Review
- Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.Biophysics and physicobiology · 2016Review
- Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.Frontiers in molecular biosciences · 2016Review
- Probing structurally altered and aggregated states of therapeutically relevant proteins using GroEL coupled to bio-layer interferometry.Protein science : a publication of the Protein Society · 2014Article
- 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
- Mechanisms of cellular proteostasis: insights from single-molecule approaches.Annual review of biophysics · 2014Review
- 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
- 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
- ATP-driven molecular chaperone machines.Biopolymers · 2013Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chaperonin, GroEL, is an essential molecular chaperone that mediates protein folding together with its cofactor, GroES, in Escherichia coli. It is widely believed that the two rings of GroEL alternate between the folding active state coupled to GroES binding during the reaction cycle. In other words, an asymmetric GroEL-GroES complex (the bullet-shaped complex) is formed throughout the cycle, whereas a symmetric GroEL-(GroES)(2) complex (the football-shaped complex) is not formed. We have recently shown that the football-shaped complex coexists with the bullet-shaped complex during the reaction cycle. However, how protein folding proceeds in the football-shaped complex remains poorly understood. Here, we used GFP as a substrate to visualize protein folding in the football-shaped complex by single-molecule fluorescence techniques. We directly showed that GFP folding occurs in both rings of the football-shaped complex. Remarkably, the folding was a sequential two-step reaction, and the kinetics were in excellent agreement with those in the bullet-shaped complex. These results demonstrate that the same reactions take place independently in both rings of the football-shaped complex to facilitate protein folding.
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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.