ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization of a paraspeckle protein PSPC1-NONO heterodimer.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 16 citations in OpenAlex.
- Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026Article
- Chromatin Meets Condensates: Emerging Interplays Linking Nuclear Paraspeckles to Gene Activation.Epigenetics reports · 2026Article
- Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1.Nucleic acids research · 2022Article
- G-quadruplexes offer a conserved structural motif for NONO recruitment to NEAT1 architectural lncRNA.Nucleic acids research · 2020Article
- Human proteins that interact with RNA/DNA hybrids.Genome research · 2018Article
- 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
- Caenorhabditis elegans NONO-1: Insights into DBHS protein structure, architecture, and function.Protein science : a publication of the Protein Society · 2015Article
- Application of array comparative genomic hybridization in 256 patients with developmental delay or intellectual disability.Journal of applied genetics · 2014Article
- Paraspeckle nuclear bodies--useful uselessness?Cellular and molecular life sciences : CMLS · 2012Review
- Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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4 authors at 1 institution in 1 country.
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Abstract
The paraspeckle component 1 (PSPC1) and non-POU-domain-containing octamer-binding protein (NONO) heterodimer is an essential structural component of paraspeckles, ribonucleoprotein bodies found in the interchromatin space of mammalian cell nuclei. PSPC1 and NONO both belong to the Drosophila behaviour and human splicing (DBHS) protein family, which has been implicated in many aspects of RNA processing. A heterodimer of the core DBHS conserved region of PSPC1 and NONO comprising two tandemly arranged RNA-recognition motifs (RRMs), a NONA/paraspeckle (NOPS) domain and part of a predicted coiled-coil domain has been crystallized in space group C2, with unit-cell parameters a = 90.90, b = 67.18, c = 94.08 Å, β = 99.96°. The crystal contained one heterodimer in the asymmetric unit and diffracted to 1.9 Å resolution using synchrotron radiation.
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