ArticlePloS one2013
ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Real-time tilting and twisting motions of ligand-bound states of α7 nicotinic acetylcholine receptor.European biophysics journal : EBJ · 2024Article
- Comparison of the Molecular Motility of Tubulin Dimeric Isoforms: Molecular Dynamics Simulations and Diffracted X-ray Tracking Study.International journal of molecular sciences · 2023Article
- Molecular Dynamics Mappings of the CCT/TRiC Complex-Mediated Protein Folding Cycle Using Diffracted X-ray Tracking.International journal of molecular sciences · 2023Article
- Diffracted X-ray Tracking for Observing the Internal Motions of Individual Protein Molecules and Its Extended Methodologies.International journal of molecular sciences · 2023Review
- Real-Time Observation of Capsaicin-Induced Intracellular Domain Dynamics of TRPV1 Using the Diffracted X-ray Tracking Method.Membranes · 2023Article
- Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022Review
- Diffracted X-ray Tracking Method for Measuring Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022Review
- CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.Nature communications · 2021Article
- Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules.Frontiers in bioinformatics · 2021Review
- Overview of "2SEA Frontiers of Synchrotron Radiation Biophysics" session of symposia in the 57th Annual Meeting of Biophysical Society of Japan.Biophysical reviews · 2020Article
- Bridging human chaperonopathies and microbial chaperonins.Communications biology · 2019Review
- Diffracted X-ray Blinking Tracks Single Protein Motions.Scientific reports · 2018Article
- Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking.International journal of molecular sciences · 2018Article
- Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC.PloS one · 2017Article
- Characterization of group II chaperonins from an acidothermophilic archaeon Picrophilus torridus.FEBS open bio · 2016Article
- The Mechanism and Function of Group II Chaperonins.Journal of molecular biology · 2015Review
- Single-molecule motions of MHC class II rely on bound peptides.Biophysical journal · 2015Article
- Real time ligand-induced motion mappings of AChBP and nAChR using X-ray single molecule tracking.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and opening of a built-in lid, which is controlled by the ATP hydrolysis cycle. Recent structural studies suggest that the ring structure of the chaperonin twists to seal off the central cavity. In this study, we demonstrate ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by diffracted X-ray tracking (DXT). A UV light-triggered DXT study with caged-ATP and stopped-flow fluorometry revealed that the lid partially closed within 1 s of ATP binding, the closed ring subsequently twisted counterclockwise within 2-6 s, as viewed from the top to bottom of the chaperonin, and the twisted ring reverted to the original open-state with a clockwise motion. Our analyses clearly demonstrate that the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion.
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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.