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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Lesne J,Locard-Paulet M,Parra J,Zivković D,Menneteau T,Bousquet MP,Burlet-Schiltz O,Marcoux Jdoi
10.1038/s41467-020-19934-zsubject
Has Abstractpub_date
2020-12-01 00:00:00pages
6140issue
1issn
2041-1723pii
10.1038/s41467-020-19934-zjournal_volume
11pub_type
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