ArticleNucleic acids research2022
Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026Article
- The paraspeckle protein NONO potentiates the antiviral innate immune response through chromatin regulation.bioRxiv : the preprint server for biology · 2026Article
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- Structural and mechanistic analysis of covalent ligands targeting the RNA-binding protein NONO.Cell chemical biology · 2026Article
- Chromatin Meets Condensates: Emerging Interplays Linking Nuclear Paraspeckles to Gene Activation.Epigenetics reports · 2026Article
- The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.Communications biology · 2025Article
- Paraspeckle protein NONO regulates active chromatin by allosterically stimulating NSD1.Cell reports · 2025Article
- Downregulation of NONO Suppresses Proliferation, Migration, and Invasion in Metastatic Prostate Cancer.The Prostate · 2025Article
- An alternative cytoplasmic SFPQ isoform with reduced phase separation potential is up-regulated in ALS.Science advances · 2025Article
- Deciphering the RNA recognition by Musashi-1 to design protein and RNA variants for in vitro and in vivo applications.Nucleic acids research · 2025Article
- Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.Acta crystallographica. Section D, Structural biology · 2025Article
- NONO, SFPQ, and PSPC1 promote telomerase recruitment to the telomere.Nature communications · 2025Article
- Spuriously transcribed RNAs from CRISPR-sgRNA expression plasmids scaffold biomolecular condensate formation and hamper accurate genomic imaging.Nucleic acids research · 2025Article
- PSPC1 exerts an oncogenic role in AML by regulating a leukemic transcription program in cooperation with PU.1.Cell stem cell · 2025Article
- Proline exacerbates hepatic gluconeogenesis via paraspeckle-dependent mRNA retention.Nature metabolism · 2025Article
- Structural plasticity of the coiled-coil interactions in human SFPQ.Nucleic acids research · 2025Article
- Paraspeckle Component 1: a multifunctional RNA binding protein.American journal of cancer research · 2025Review
- PROSER1 modulates DNA demethylation through dual mechanisms to prevent syndromic developmental malformations.Genes & development · 2024Article
- Role of RNA binding proteins of theRNA biology · 2024Review
- A DBHS family member regulates male determination in the filariasis vector Armigeres subalbatus.Nature communications · 2023Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Drosophila behaviour/human splicing (DBHS) proteins are a family of RNA/DNA binding cofactors liable for a range of cellular processes. DBHS proteins include the non-POU domain-containing octamer-binding protein (NONO) and paraspeckle protein component 1 (PSPC1), proteins capable of forming combinatorial dimers. Here, we describe the crystal structures of the human NONO and PSPC1 homodimers, representing uncharacterized DBHS dimerization states. The structures reveal a set of conserved contacts and structural plasticity within the dimerization interface that provide a rationale for dimer selectivity between DBHS paralogues. In addition, solution X-ray scattering and accompanying biochemical experiments describe a mechanism of cooperative RNA recognition by the NONO homodimer. Nucleic acid binding is reliant on RRM1, and appears to be affected by the orientation of RRM1, influenced by a newly identified 'β-clasp' structure. Our structures shed light on the molecular determinants for DBHS homo- and heterodimerization and provide a basis for understanding how DBHS proteins cooperatively recognize a broad spectrum of RNA targets.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.