---
_id: '10323'
abstract:
- lang: eng
text: Molecular chaperones are central to cellular protein homeostasis. Dynamic
disorder is a key feature of the complexes of molecular chaperones and their client
proteins, and it facilitates the client release towards a folded state or the
handover to downstream components. The dynamic nature also implies that a given
chaperone can interact with many different client proteins, based on physico-chemical
sequence properties rather than on structural complementarity of their (folded)
3D structure. Yet, the balance between this promiscuity and some degree of client
specificity is poorly understood. Here, we review recent atomic-level descriptions
of chaperones with client proteins, including chaperones in complex with intrinsically
disordered proteins, with membrane-protein precursors, or partially folded client
proteins. We focus hereby on chaperone-client interactions that are independent
of ATP. The picture emerging from these studies highlights the importance of dynamics
in these complexes, whereby several interaction types, not only hydrophobic ones,
contribute to the complex formation. We discuss these features of chaperone-client
complexes and possible factors that may contribute to this balance of promiscuity
and specificity.
acknowledgement: We thank Juan C. Fontecilla-Camps for insightful discussions related
to ATP-driven machineries, and Elif Karagöz for providing the structural model of
the Hsp90-Tau complex. This study was supported by the European Research Council
(StG-2012-311318-ProtDyn2Function) and the Agence Nationale de la Recherche (ANR-18-CE92-0032-MitoMemProtImp).
article_number: '762005'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Iva
full_name: Sučec, Iva
last_name: Sučec
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client
proteins? Frontiers in Molecular Biosciences. 2021;8. doi:10.3389/fmolb.2021.762005
apa: Sučec, I., Bersch, B., & Schanda, P. (2021). How do chaperones bind (partly)
unfolded client proteins? Frontiers in Molecular Biosciences. Frontiers.
https://doi.org/10.3389/fmolb.2021.762005
chicago: Sučec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly)
Unfolded Client Proteins?” Frontiers in Molecular Biosciences. Frontiers,
2021. https://doi.org/10.3389/fmolb.2021.762005.
ieee: I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded
client proteins?,” Frontiers in Molecular Biosciences, vol. 8. Frontiers,
2021.
ista: Sučec I, Bersch B, Schanda P. 2021. How do chaperones bind (partly) unfolded
client proteins? Frontiers in Molecular Biosciences. 8, 762005.
mla: Sučec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?”
Frontiers in Molecular Biosciences, vol. 8, 762005, Frontiers, 2021, doi:10.3389/fmolb.2021.762005.
short: I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).
date_created: 2021-11-21T23:01:29Z
date_published: 2021-10-25T00:00:00Z
date_updated: 2023-08-14T11:55:04Z
day: '25'
ddc:
- '547'
department:
- _id: PaSc
doi: 10.3389/fmolb.2021.762005
external_id:
isi:
- '000717241700001'
pmid:
- '34760928'
file:
- access_level: open_access
checksum: a5c9dbf80dc2c5aaa737f456c941d964
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-23T15:06:58Z
date_updated: 2021-11-23T15:06:58Z
file_id: '10333'
file_name: 2021_FrontiersMolBioSc_Sučec.pdf
file_size: 4700798
relation: main_file
success: 1
file_date_updated: 2021-11-23T15:06:58Z
has_accepted_license: '1'
intvolume: ' 8'
isi: 1
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: Frontiers in Molecular Biosciences
publication_identifier:
eissn:
- 2296-889X
publication_status: published
publisher: Frontiers
quality_controlled: '1'
scopus_import: '1'
status: public
title: How do chaperones bind (partly) unfolded client proteins?
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 8
year: '2021'
...