Journal Article

DZNE-2022-01516

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Molecular interactions of FG nucleoporin repeats at high resolution.

Ibanez de Opakua, A. (First author)DZNE* ; Geraets, J. A. ; Frieg, B. ; Dienemann, C. ; Savastano, A.DZNE* ; Rankovic, M.Extern* ; Cima-Omori, M.-S. ; Schröder, G. F. ; Zweckstetter, M. (Last author)DZNE*

2022
Nature Publishing Group London

This record in other databases:    

Please use a persistent id in citations: doi:10.1038/s41557-022-01035-7

Abstract: Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient β-structure and a stable preformed α-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG-FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities.

Keyword(s): Humans (MeSH) ; Cryoelectron Microscopy (MeSH) ; Nuclear Pore: chemistry (MeSH) ; Nuclear Pore: metabolism (MeSH) ; Nuclear Pore Complex Proteins: genetics (MeSH) ; Nuclear Pore Complex Proteins: analysis (MeSH) ; Nuclear Pore Complex Proteins: chemistry (MeSH) ; Phenylalanine: chemistry (MeSH) ; Repetitive Sequences, Amino Acid (MeSH) ; Nuclear Pore Complex Proteins ; Phenylalanine ; Nup98 protein, human

Note: CC BY: https://creativecommons.org/licenses/by/4.0/

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Contributing Institute(s):

1. Structural Biology in Dementia (AG Zweckstetter)

Research Program(s):

1. 352 - Disease Mechanisms (POF4-352) (POF4-352)

Appears in the scientific report 2022

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Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Chemical Reactions ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 20 ; Index Chemicus ; JCR ; Nationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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Linked articles:

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dataset Ibanez de Opakua, A.DZNE* ; Geraets, J.
Dataset: Cryo-em structure of the Nup98 fibril polymorph 3 (EMD-13853)
Electron Microscopy Data Bank (EMDB) (2022)2022   Fulltext BibTeX | EndNote: XML, Text | RIS

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dataset Ibanez de Opakua, A.DZNE* ; Geraets, J.
Cryo-em structure of the Nup98 fibril polymorph 4 (EMD-13854)
Electron Microscopy Data Bank (EMDB) (2022)2022   Fulltext BibTeX | EndNote: XML, Text | RIS

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dataset Ibanez de Opakua, A.DZNE* ; Geraets, J.
Cryo-em structure of the Nup98 fibril polymorph 2 (EMD-13852)
Electron Microscopy Data Bank (EMDB) (2022)2022   Fulltext BibTeX | EndNote: XML, Text | RIS

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dataset Ibanez de Opakua, A.DZNE* ; Geraets, J.
Cryo-em structure of the Nup98 fibril polymorph 1 (EMD-13851)
Electron Microscopy Data Bank (EMDB) (2022)2022   Fulltext BibTeX | EndNote: XML, Text | RIS

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