eprintid: 10116858
rev_number: 14
eprint_status: archive
userid: 608
dir: disk0/10/11/68/58
datestamp: 2020-12-09 17:12:19
lastmod: 2021-10-09 23:07:29
status_changed: 2020-12-09 17:12:19
type: article
metadata_visibility: show
creators_name: Lesne, J
creators_name: Locard-Paulet, M
creators_name: Parra, J
creators_name: Zivković, D
creators_name: Menneteau, T
creators_name: Bousquet, M-P
creators_name: Burlet-Schiltz, O
creators_name: Marcoux, J
title: Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalks
ispublished: pub
divisions: UCL
divisions: B02
divisions: C08
divisions: D09
divisions: G03
keywords: Mass spectrometry, Proteasome, Structural biology, Supramolecular assembly
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abstract: Hydrogen-Deuterium eXchange coupled to Mass Spectrometry (HDX-MS) is now common practice in structural biology. However, it is most of the time applied to rather small oligomeric complexes. Here, we report on the use of HDX-MS to investigate conformational differences between the human standard 20S (std20S) and immuno 20S (i20s) proteasomes alone or in complex with PA28αβ or PA28γ activators. Their solvent accessibility is analyzed through a dedicated bioinformatic pipeline including stringent statistical analysis and 3D visualization. These data confirm the existence of allosteric differences between the std20S and i20S at the surface of the α-ring triggered from inside the catalytic β-ring. Additionally, binding of the PA28 regulators to the 20S proteasomes modify solvent accessibility due to conformational changes of the β-rings. This work is not only a proof-of-concept that HDX-MS can be used to get structural insights on large multi-protein complexes in solution, it also demonstrates that the binding of the std20S or i20S subtype to any of its PA28 activator triggers allosteric changes that are specific to this 20S/PA28 pair.
date: 2020-12-01
date_type: published
official_url: https://doi.org/10.1038/s41467-020-19934-z
oa_status: green
full_text_type: pub
language: eng
primo: open
primo_central: open_green
verified: verified_manual
elements_id: 1833886
doi: 10.1038/s41467-020-19934-z
pii: 10.1038/s41467-020-19934-z
lyricists_name: Menneteau, Thomas
lyricists_id: TMENN45
actors_name: Austen, Jennifer
actors_id: JAUST66
actors_role: owner
full_text_status: public
publication: Nature Communications
volume: 11
article_number: 6140
event_location: England
citation:        Lesne, J;    Locard-Paulet, M;    Parra, J;    Zivković, D;    Menneteau, T;    Bousquet, M-P;    Burlet-Schiltz, O;           Lesne, J;  Locard-Paulet, M;  Parra, J;  Zivković, D;  Menneteau, T;  Bousquet, M-P;  Burlet-Schiltz, O;  Marcoux, J;   - view fewer <#>    (2020)    Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalks.                   Nature Communications , 11     , Article 6140.  10.1038/s41467-020-19934-z <https://doi.org/10.1038/s41467-020-19934-z>.       Green open access   
 
document_url: https://discovery.ucl.ac.uk/id/eprint/10116858/1/s41467-020-19934-z.pdf