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TitleImpact of distinct FG nucleoporin repeats on Nup98 self-association.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3797, Year 2024
Publish dateMay 7, 2024
AuthorsAlain Ibáñez de Opakua / Christian F Pantoja / Maria-Sol Cima-Omori / Christian Dienemann / Markus Zweckstetter /
PubMed AbstractNucleoporins rich in phenylalanine/glycine (FG) residues form the permeability barrier within the nuclear pore complex and are implicated in several pathological cellular processes, including ...Nucleoporins rich in phenylalanine/glycine (FG) residues form the permeability barrier within the nuclear pore complex and are implicated in several pathological cellular processes, including oncogenic fusion condensates. The self-association of FG-repeat proteins and interactions between FG-repeats play a critical role in these activities by forming hydrogel-like structures. Here we show that mutation of specific FG repeats of Nup98 can strongly decrease the protein's self-association capabilities. We further present a cryo-electron microscopy structure of a Nup98 peptide fibril with higher stability per residue compared with previous Nup98 fibril structures. The high-resolution structure reveals zipper-like hydrophobic patches which contain a GLFG motif and are less compatible for binding to nuclear transport receptors. The identified distinct molecular properties of different regions of the nucleoporin may contribute to spatial variations in the self-association of FG-repeats, potentially influencing transport processes through the nuclear pore.
External linksNat Commun / PubMed:38714656 / PubMed Central
MethodsEM (helical sym.)
Resolution2.67 Å
Structure data

16671

8ci8

EMDB-16671, PDB-8ci8:
Cryo-EM structure of the Nup98(298-327) fibril
Method: EM (helical sym.) / Resolution: 2.67 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Nup98 / nuclear pore / FG repeats / amyloid fibrils

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