Journal Article

FZJ-2022-05457

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

Ibáñez de Opakua, A. ; Geraets, J.FZJ* ; Frieg, B.FZJ* ; Dienemann, C. ; Savastano, A. ; Rankovic, M. ; Cima-Omori, M.-S. ; Schröder, G. F. (Corresponding author)FZJ* ; Zweckstetter, M. (Corresponding author)

2022
Nature Publishing Group London

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Please use a persistent id in citations: http://hdl.handle.net/2128/33449  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.

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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 5244 - Information Processing in Neuronal Networks (POF4-524) (POF4-524)

Appears in the scientific report 2022

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Database coverage:
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