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| Title | The gene-regulating proteins NONO and SFPQ assemble into ordered filaments. |
|---|---|
| Journal, issue, pages | Commun Biol, Vol. 9, Issue 1, Page 117, Year 2025 |
| Publish date | Dec 31, 2025 |
Authors | Tim Rasmussen / Jannik Küspert / Lars Schönemann / Dietmar Geiger / Bettina Böttcher / ![]() |
| PubMed Abstract | Proteins of the Drosophila behaviour/human splicing (DBHS) family are involved in many aspects of gene regulation and maintenance like transcription, splicing and DNA repair. DBHS proteins form ...Proteins of the Drosophila behaviour/human splicing (DBHS) family are involved in many aspects of gene regulation and maintenance like transcription, splicing and DNA repair. DBHS proteins form obligate homo- and heterodimers through interactions within a globular domain and can further dynamically oligomerise through α-helical coiled-coils, which is crucial for many functions. While the atomic structures of the dimers are established, the arrangement in higher oligomers is unknown. Here we present the structure of a filamentous NONO/SFPQ heterooligomer resolved by cryo-EM. The filaments form a double helix which is stabilized by an interdigitating network of coiled-coil interactions. |
External links | Commun Biol / PubMed:41476260 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.3 - 3.9 Å |
| Structure data | ![]() EMDB-51413: NONO/SFPQ filament, overall map ![]() EMDB-51417: NONO/SFPQ filament: local refinement single strand (strand 1) ![]() EMDB-51418: NONO/SFPQ filament: local refinment single strand (strand 2) EMDB-51438, PDB-9glc: EMDB-51439, PDB-9gld: EMDB-51471, PDB-9gni: |
| Source |
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Keywords | NUCLEAR PROTEIN / filament / RNA binding / DNA binding / gene regulation |
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