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Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle

The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar subunits arranged in two stacked rings. Substrate folding inside the central chamber is triggered by ATP hydrolysis. We present five cryo-EM structures of TRiC in apo and nucleotide-induced states wit...

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Autores principales: Cong, Yao, Schröder, Gunnar F, Meyer, Anne S, Jakana, Joanita, Ma, Boxue, Dougherty, Matthew T, Schmid, Michael F, Reissmann, Stefanie, Levitt, Michael, Ludtke, Steven L, Frydman, Judith, Chiu, Wah
Formato: Online Artículo Texto
Lenguaje:English
Publicado: European Molecular Biology Organization 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3273382/
https://www.ncbi.nlm.nih.gov/pubmed/22045336
http://dx.doi.org/10.1038/emboj.2011.366
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author Cong, Yao
Schröder, Gunnar F
Meyer, Anne S
Jakana, Joanita
Ma, Boxue
Dougherty, Matthew T
Schmid, Michael F
Reissmann, Stefanie
Levitt, Michael
Ludtke, Steven L
Frydman, Judith
Chiu, Wah
author_facet Cong, Yao
Schröder, Gunnar F
Meyer, Anne S
Jakana, Joanita
Ma, Boxue
Dougherty, Matthew T
Schmid, Michael F
Reissmann, Stefanie
Levitt, Michael
Ludtke, Steven L
Frydman, Judith
Chiu, Wah
author_sort Cong, Yao
collection PubMed
description The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar subunits arranged in two stacked rings. Substrate folding inside the central chamber is triggered by ATP hydrolysis. We present five cryo-EM structures of TRiC in apo and nucleotide-induced states without imposing symmetry during the 3D reconstruction. These structures reveal the intra- and inter-ring subunit interaction pattern changes during the ATPase cycle. In the apo state, the subunit arrangement in each ring is highly asymmetric, whereas all nucleotide-containing states tend to be more symmetrical. We identify and structurally characterize an one-ring closed intermediate induced by ATP hydrolysis wherein the closed TRiC ring exhibits an observable chamber expansion. This likely represents the physiological substrate folding state. Our structural results suggest mechanisms for inter-ring-negative cooperativity, intra-ring-positive cooperativity, and protein-folding chamber closure of TRiC. Intriguingly, these mechanisms are different from other group I and II chaperonins despite their similar architecture.
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spelling pubmed-32733822012-02-06 Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle Cong, Yao Schröder, Gunnar F Meyer, Anne S Jakana, Joanita Ma, Boxue Dougherty, Matthew T Schmid, Michael F Reissmann, Stefanie Levitt, Michael Ludtke, Steven L Frydman, Judith Chiu, Wah EMBO J Article The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar subunits arranged in two stacked rings. Substrate folding inside the central chamber is triggered by ATP hydrolysis. We present five cryo-EM structures of TRiC in apo and nucleotide-induced states without imposing symmetry during the 3D reconstruction. These structures reveal the intra- and inter-ring subunit interaction pattern changes during the ATPase cycle. In the apo state, the subunit arrangement in each ring is highly asymmetric, whereas all nucleotide-containing states tend to be more symmetrical. We identify and structurally characterize an one-ring closed intermediate induced by ATP hydrolysis wherein the closed TRiC ring exhibits an observable chamber expansion. This likely represents the physiological substrate folding state. Our structural results suggest mechanisms for inter-ring-negative cooperativity, intra-ring-positive cooperativity, and protein-folding chamber closure of TRiC. Intriguingly, these mechanisms are different from other group I and II chaperonins despite their similar architecture. European Molecular Biology Organization 2012-02-01 2011-11-01 /pmc/articles/PMC3273382/ /pubmed/22045336 http://dx.doi.org/10.1038/emboj.2011.366 Text en Copyright © 2012, European Molecular Biology Organization https://creativecommons.org/licenses/by-nc-sa/3.0/This is an open-access article distributed under the terms of the Creative Commons Attribution Noncommercial Share Alike 3.0 Unported License, which allows readers to alter, transform, or build upon the article and then distribute the resulting work under the same or similar license to this one. The work must be attributed back to the original author and commercial use is not permitted without specific permission.
spellingShingle Article
Cong, Yao
Schröder, Gunnar F
Meyer, Anne S
Jakana, Joanita
Ma, Boxue
Dougherty, Matthew T
Schmid, Michael F
Reissmann, Stefanie
Levitt, Michael
Ludtke, Steven L
Frydman, Judith
Chiu, Wah
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
title Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
title_full Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
title_fullStr Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
title_full_unstemmed Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
title_short Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
title_sort symmetry-free cryo-em structures of the chaperonin tric along its atpase-driven conformational cycle
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3273382/
https://www.ncbi.nlm.nih.gov/pubmed/22045336
http://dx.doi.org/10.1038/emboj.2011.366
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