2014
DOI: 10.1016/j.jmb.2013.09.034
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Dissection of the ATP-Dependent Conformational Change Cycle of a Group II Chaperonin

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Cited by 12 publications
(12 citation statements)
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“…In our previous study using TKS1-Cpn [20, 21], the binding of ATP induced a conformational change in each subunit within 1 s. The conformational change appeared as a tilting motion toward the center of the cavity, and it caused TKS1-Cpn to have a partially closed conformation. At this stage, the closure degree of TKS1-Cpn was not enough for protein folding because the substrate was still bound to the TKS1-Cpn subunit and was not released toward the cavity.…”
Section: Discussionmentioning
confidence: 99%
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“…In our previous study using TKS1-Cpn [20, 21], the binding of ATP induced a conformational change in each subunit within 1 s. The conformational change appeared as a tilting motion toward the center of the cavity, and it caused TKS1-Cpn to have a partially closed conformation. At this stage, the closure degree of TKS1-Cpn was not enough for protein folding because the substrate was still bound to the TKS1-Cpn subunit and was not released toward the cavity.…”
Section: Discussionmentioning
confidence: 99%
“…Compared to the apostate conformation, the apical domains of ATP-bound subunits were rotated by approximately 45°. Detailed kinetic studies have been performed using chaperonins from Thermococcus strain KS-1 (TKS1-Cpn) [20]. A UV light-triggered diffracted X-ray tracking (DXT) study with caged-ATP and stopped-flow fluorometry revealed that the lid was partially closed within 1 s after ATP binding, and the closed ring subsequently twisted counterclockwise within 2–6 s, as viewed from the top to bottom of TKS1-Cpn, and the twisted ring reverted to the original open state with a clockwise motion [21].…”
Section: Introductionmentioning
confidence: 99%
“…Molecular chaperones are indispensable cellular components that assist folding and assembly of newly synthesized proteins, translocation of proteins across membranes, as well as refolding and degrading of misfolded and aggregated proteins 1 . A class of chaperones, the chaperonins (Cpns) are large, hollow, ATP-dependent nanomachines that promote correct folding of a wide range of proteins 2 3 4 5 6 7 . Cpns are divided into two groups: group I Cpns, represented by GroEL/GroES, in bacteria, mitochondria and chloroplasts, and group II Cpns, occurring in eukaryotes and archaea 8 9 10 .…”
mentioning
confidence: 99%
“…On the basis of these results, we showed that T . KS1 CPN in the absence of nucleotides is in the relatively flexible state, and ATP‐binding first fixed it in the open conformation, and a conformational change was induced into the closed form . It is possible that the difference in the ability to arrest GFP refolding between 30 and 50 °C might be due to the difference in the flexibility of the conformation.…”
Section: Resultsmentioning
confidence: 99%
“…KS1 CPN) exhibit relatively high in vitro protein folding ability and structural stability. We also revealed the detailed mechanisms for the conformational change and protein folding of group II CPNs .…”
mentioning
confidence: 99%