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Protein interfaces of the conserved Nup84 complex from Chaetomium thermophilum shown by crosslinking mass spectrometry and electron microscopy

A key building block of the nuclear pore complex (NPC) is the Nup84 subcomplex that has been structurally analyzed predominantly in the yeast system. To expand this analysis and gain insight into the evolutionary conservation of its structure, we reconstituted an octameric Nup84 complex using the su...

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Hauptverfasser: Thierbach, Karsten (Verfasst von) , Appen, Alexander von (Verfasst von) , Thoms, Matthias (Verfasst von) , Beck, Martin (Verfasst von) , Flemming, Dirk (Verfasst von) , Hurt, Ed (Verfasst von)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: August 15, 2013
In: Structure
Year: 2013, Jahrgang: 21, Heft: 9, Pages: 1672-1682
ISSN:1878-4186
DOI:10.1016/j.str.2013.07.004
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.str.2013.07.004
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0969212613002530
Volltext
Verfasserangaben:Karsten Thierbach, Alexander von Appen, Matthias Thoms, Martin Beck, Dirk Flemming, and Ed Hurt
Beschreibung
Zusammenfassung:A key building block of the nuclear pore complex (NPC) is the Nup84 subcomplex that has been structurally analyzed predominantly in the yeast system. To expand this analysis and gain insight into the evolutionary conservation of its structure, we reconstituted an octameric Nup84 complex using the subunits from a thermophile, Chaetomium thermophilum (ct). This assembly carries Nup37 and Elys, which are characteristic subunits of the orthologous human Nup107-Nup160 complex but absent from the yeast Saccharomyces cerevisiae. We found that Elys binds cooperatively to the complex requiring both Nup37 and Nup120. Unexpectedly, the reconstituted ctNup84 complex formed a striking dimer structure with an unpredicted side-to-side arrangement of two molecules. Finally, crosslinking mass spectrometry allowed the mapping of key protein interfaces within the Y-shaped complex. Thus, the thermophilic Nup84 complex can serve as a structural model for higher eukaryotic Nup107-Nup160 assemblies to gain insight into its possible configuration within the NPC scaffold.
Beschreibung:Gesehen am 03.02.2022
Beschreibung:Online Resource
ISSN:1878-4186
DOI:10.1016/j.str.2013.07.004

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