ArticleThe Journal of biological chemistry2010
Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Zero-mode waveguides and nanopore-based sequencing technologies accelerate single-molecule studies.Biophysics and physicobiology · 2022Article
- Fast interaction dynamics of G-quadruplex and RGG-rich peptides unveiled in zero-mode waveguides.Nucleic acids research · 2021Article
- 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
- Article
- Monitoring the Waiting Time Sequence of Single Ras GTPase Activation Events Using Liposome Functionalized Zero-Mode Waveguides.Nano letters · 2016Article
- 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
- Synergistic effect of ATP for RuvA-RuvB-Holliday junction DNA complex formation.Scientific reports · 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
- How do chaperonins fold protein?Biophysics (Nagoya-shi, Japan) · 2015Review
- smFRET studies of the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand binding.FEBS letters · 2014Review
- 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
- High-throughput platform for real-time monitoring of biological processes by multicolor single-molecule fluorescence.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dark-field illumination on zero-mode waveguide/microfluidic hybrid chip reveals T4 replisomal protein interactions.Nano letters · 2014Article
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
- Robustly passivated, gold nanoaperture arrays for single-molecule fluorescence microscopy.ACS nano · 2013Article
- Lab-on-a-chip technologies for single-molecule studies.Lab on a chip · 2013Article
- Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been widely believed that an asymmetric GroEL-GroES complex (termed the bullet-shaped complex) is formed solely throughout the chaperonin reaction cycle, whereas we have recently revealed that a symmetric GroEL-(GroES)(2) complex (the football-shaped complex) can form in the presence of denatured proteins. However, the dynamics of the GroEL-GroES interaction, including the football-shaped complex, is unclear. We investigated the decay process of the football-shaped complex at a single-molecule level. Because submicromolar concentrations of fluorescent GroES are required in solution to form saturated amounts of the football-shaped complex, single-molecule fluorescence imaging was carried out using zero-mode waveguides. The single-molecule study revealed two insights into the GroEL-GroES reaction. First, the first GroES to interact with GroEL does not always dissociate from the football-shaped complex prior to the dissociation of a second GroES. Second, there are two cycles, the "football cycle " and the "bullet cycle," in the chaperonin reaction, and the lifetimes of the football-shaped and the bullet-shaped complexes were determined to be 3-5 s and about 6 s, respectively. These findings shed new light on the molecular mechanism of protein folding mediated by the GroEL-GroES chaperonin system.
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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.