The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.

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.

SUBMITTER: Rasmussen T 

PROVIDER: S-EPMC12848012 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature