ArticleProtein science : a publication of the Protein Society2015
Caenorhabditis elegans NONO-1: Insights into DBHS protein structure, architecture, and function.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026Article
- The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.Communications biology · 2025Article
- Review
- Structural plasticity of the coiled-coil interactions in human SFPQ.Nucleic acids research · 2025Article
- Established and Evolving Roles of the Multifunctional Non-POU Domain-Containing Octamer-Binding Protein (NonO) and Splicing Factor Proline- and Glutamine-Rich (SFPQ).Journal of developmental biology · 2024Review
- A DBHS family member regulates male determination in the filariasis vector Armigeres subalbatus.Nature communications · 2023Article
- NONO enhances mRNA processing of super-enhancer-associated GATA2 and HAND2 genes in neuroblastoma.EMBO reports · 2023Article
- Molecular Modelling of NONO and SFPQ Dimerization Process and RNA Recognition Mechanism.International journal of molecular sciences · 2022Article
- Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1.Nucleic acids research · 2022Article
- Article
- The RNA-binding protein SFPQ preserves long-intron splicing and regulates circRNA biogenesis in mammals.eLife · 2021Article
- NONO and tumorigenesis: More than splicing.Journal of cellular and molecular medicine · 2020Review
- A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Crystal structure of a SFPQ/PSPC1 heterodimer provides insights into preferential heterodimerization of human DBHS family proteins.The Journal of biological chemistry · 2018Article
- SFPQ•NONO and XLF function separately and together to promote DNA double-strand break repair via canonical nonhomologous end joining.Nucleic acids research · 2017Article
- A crystallographic study of human NONO (p54(nrb)): overcoming pathological problems with purification, data collection and noncrystallographic symmetry.Acta crystallographica. Section D, Structural biology · 2016Article
- The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.Nucleic acids research · 2016Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the Drosophila behavior/human splicing (DBHS) protein family have been characterized in the vertebrates Homo sapiens and Mus musculus, and the invertebrates Drosophila melanogaster and Chironomus tentans. Collectively, both vertebrate and invertebrate DBHS proteins function throughout gene regulation, largely but not always, within the nucleus. In this study, we report a structural and bioinformatic analysis of the DBHS protein family to guide future studies into DBHS protein function. To explore the structural plasticity of the family, we describe the 2.4 Å crystal structure of Caenorhabditis elegans non-POU domain-containing octamer-binding protein 1 (NONO-1). The structure is dimeric, with a domain arrangement consistent with mammalian DBHS proteins. Comparison with the DBHS structures available from H. sapiens reveals that there is inherent domain flexibility within the homologous DBHS region. Mapping amino acid similarity within the family to the NONO-1 dimer highlights the dimer interface, coiled-coil oligomerization motif, and putative RNA binding surfaces. Surprisingly, the interior surface of RNA recognition motif 2 (RRM2) that faces a large internal void is highly variable, but the external β2-β3 loops of RRM2 show remarkable preservation. Overall, the DBHS region is under strong purifying selection, whereas the sequences N- and C-terminal to the DBHS region are less constrained. The findings described in this study provide a molecular basis for further investigation into the mechanistic function of the DBHS protein family in biology.
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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.