9GNI

NONO/SFPQ filament: composite structure

This is a non-PDB format compatible entry.

Summary for 9GNI

• Entry DOI: 10.2210/pdb9gni/pdb
• Related: 9GLC 9GLD
• EMDB information: 51471
• Descriptor: Splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated), Non-POU domain-containing octamer-binding protein isoform X2 (2 entities in total)
• Functional Keywords: filament, rna binding, dna binding, gene regulation, nuclear protein
• Biological source: Cricetulus griseus (Chinese hamster); More
• Total number of polymer chains: 32
• Total formula weight: 2086399.74

Authors

Rasmussen, T.,Bottcher, B. (deposition date: 2024-09-03, release date: 2025-09-17, Last modification date: 2026-03-11)

Primary citation

Rasmussen, T.,Kuspert, J.,Schonemann, L.,Geiger, D.,Bottcher, B.
The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.
Commun Biol, 9:117-117, 2025

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 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.

PubMed: 41476260
DOI: 10.1038/s42003-025-09396-8

Experimental method

ELECTRON MICROSCOPY (3.9 Å)