---
_id: '8437'
abstract:
- lang: eng
text: Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota,
and archaea, facilitating the folding of proteins, preventing protein aggregation,
and thus participating in maintaining protein homeostasis in the cell. During
their functional cycle, they bind unfolded client proteins inside their double
ring structure and promote protein folding by closing the ring chamber in an adenosine
5′-triphosphate (ATP)–dependent manner. Although the static structures of fully
open and closed forms of chaperonins were solved by x-ray crystallography or electron
microscopy, elucidating the mechanisms of such ATP-driven molecular events requires
studying the proteins at the structural level under working conditions. We introduce
an approach that combines site-specific nuclear magnetic resonance observation
of very large proteins, enabled by advanced isotope labeling methods, with an
in situ ATP regeneration system. Using this method, we provide functional insight
into the 1-MDa large hsp60 chaperonin while processing client proteins and reveal
how nucleotide binding, hydrolysis, and release control switching between closed
and open states. While the open conformation stabilizes the unfolded state of
client proteins, the internalization of the client protein inside the chaperonin
cavity speeds up its functional cycle. This approach opens new perspectives to
study structures and mechanisms of various ATP-driven biological machineries in
the heat of action.
article_number: eaau4196
article_processing_charge: No
article_type: original
author:
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jia-Ying
full_name: Guan, Jia-Ying
last_name: Guan
- first_name: Elodie
full_name: Crublet, Elodie
last_name: Crublet
- first_name: Elisa Colas
full_name: Debled, Elisa Colas
last_name: Debled
- first_name: Christine
full_name: Moriscot, Christine
last_name: Moriscot
- first_name: Pierre
full_name: Gans, Pierre
last_name: Gans
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin
in action reveals how nucleotide binding regulates the functional cycle. Science
Advances. 2018;4(9). doi:10.1126/sciadv.aau4196
apa: Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., …
Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals
how nucleotide binding regulates the functional cycle. Science Advances.
American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aau4196
chicago: Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine
Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier.
“Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding
Regulates the Functional Cycle.” Science Advances. American Association
for the Advancement of Science, 2018. https://doi.org/10.1126/sciadv.aau4196.
ieee: G. Mas et al., “Structural investigation of a chaperonin in action
reveals how nucleotide binding regulates the functional cycle,” Science Advances,
vol. 4, no. 9. American Association for the Advancement of Science, 2018.
ista: Mas G, Guan J-Y, Crublet E, Debled EC, Moriscot C, Gans P, Schoehn G, Macek
P, Schanda P, Boisbouvier J. 2018. Structural investigation of a chaperonin in
action reveals how nucleotide binding regulates the functional cycle. Science
Advances. 4(9), eaau4196.
mla: Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action
Reveals How Nucleotide Binding Regulates the Functional Cycle.” Science Advances,
vol. 4, no. 9, eaau4196, American Association for the Advancement of Science,
2018, doi:10.1126/sciadv.aau4196.
short: G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn,
P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).
date_created: 2020-09-18T10:04:51Z
date_published: 2018-09-19T00:00:00Z
date_updated: 2022-08-26T09:11:06Z
day: '19'
doi: 10.1126/sciadv.aau4196
extern: '1'
intvolume: ' 4'
issue: '9'
language:
- iso: eng
month: '09'
oa_version: None
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
status: public
title: Structural investigation of a chaperonin in action reveals how nucleotide binding
regulates the functional cycle
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 4
year: '2018'
...