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-Structure paper
タイトル | Molecular interactions of FG nucleoporin repeats at high resolution. |
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ジャーナル・号・ページ | Nat Chem, Vol. 14, Issue 11, Page 1278-1285, Year 2022 |
掲載日 | 2022年9月22日 |
著者 | Alain Ibáñez de Opakua / James A Geraets / Benedikt Frieg / Christian Dienemann / Adriana Savastano / Marija Rankovic / Maria-Sol Cima-Omori / Gunnar F Schröder / Markus Zweckstetter / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Chem / PubMed:36138110 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.76 - 3.37 Å |
構造データ | EMDB-13851, PDB-7q64: EMDB-13852, PDB-7q65: EMDB-13853, PDB-7q66: EMDB-13854, PDB-7q67: |
由来 |
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キーワード | PROTEIN FIBRIL / Nuclear pore complex protein Nup98 functional amyloid fibril PROTEIN FIBRIL |