ArticleThe EMBO journal1995
snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 1 of them a synthesis that pooled it.
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Who cites it
103 citing papers in PubMed, 1 synthesis or guideline pooled it, 249 citations in OpenAlex.
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- The Arabidopsis thaliana core splicing factor PORCUPINE/SmE1 requires intron-mediated expression.PloS one · 2025Article
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- The diagnostic and prognostic significance of small nuclear ribonucleoprotein Sm D1 aberrantly high expression in hepatocellular carcinoma.Journal of Cancer · 2022Article
- Genes for RNA-binding proteins involved in neural-specific functions and diseases are downregulated in Rubinstein-Taybi iNeurons.Neural regeneration research · 2022Article
- A survey of protein interactions and posttranslational modifications that influence the polyglutamine diseases.Frontiers in molecular neuroscience · 2022Review
- Anti-Sm antibodies in the classification criteria of systemic lupus erythematosus.Journal of translational autoimmunity · 2022Article
- Nucleoid-associated proteins shape chromatin structure and transcriptional regulation across the bacterial kingdom.Transcription · 2021Review
- Biology of the mRNA Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities.International journal of molecular sciences · 2021Review
- Core spliceosomal Sm proteins as constituents of cytoplasmic mRNPs in plants.The Plant journal : for cell and molecular biology · 2020Article
- Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites.Nucleic acids research · 2020Article
- Composition and processing activity of a semi-recombinant holo U7 snRNP.Nucleic acids research · 2020Article
- Clinical Significance, Cellular Function, and Potential Molecular Pathways of CCT7 in Endometrial Cancer.Frontiers in oncology · 2020Article
- Article
- Arabidopsis SME1 Regulates Plant Development and Response to Abiotic Stress by Determining Spliceosome Activity Specificity.The Plant cell · 2019Article
- The oncogenic potential of small nuclear ribonucleoprotein polypeptide G: a comprehensive and perspective view.American journal of translational research · 2019Review
- Emerging Roles of LSM Complexes in Posttranscriptional Regulation of Plant Response to Abiotic Stress.Frontiers in plant science · 2019Review
- UsnRNP biogenesis: mechanisms and regulation.Chromosoma · 2017Review
43 more citing papers are in PubMed but not listed here.
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spliceosomal small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/U6 and U5 share eight proteins B', B, D1, D2, D3, E, F and G which form the structural core of the snRNPs. This class of common proteins plays an essential role in the biogenesis of the snRNPs. In addition, these proteins represent the major targets for the so-called anti-Sm auto-antibodies which are diagnostic for systemic lupus erythematosus (SLE). We have characterized the proteins F and G from HeLa cells by cDNA cloning, and, thus, all human Sm protein sequences are now available for comparison. Similar to the D, B/B' and E proteins, the F and G proteins do not possess any of the known RNA binding motifs, suggesting that other types of RNA-protein interactions occur in the snRNP core. Strikingly, the eight human Sm proteins possess mutual homology in two regions, 32 and 14 amino acids long, that we term Sm motifs 1 and 2. The Sm motifs are evolutionarily highly conserved in all of the putative homologues of the human Sm proteins identified in the data base. These results suggest that the Sm proteins may have arisen from a single common ancestor. Several hypothetical proteins, mainly of plant origin, that clearly contain the conserved Sm motifs but exhibit only comparatively low overall homology to one of the human Sm proteins, were identified in the data base. This suggests that the Sm motifs may also be shared by non-spliceosomal proteins. Further, we provide experimental evidence that the Sm motifs are involved, at least in part, in Sm protein-protein interactions. Specifically, we show by co-immunoprecipitation analyses of in vitro translated B' and D3 that the Sm motifs are essential for complex formation between B' and D3. Our finding that the Sm proteins share conserved sequence motifs may help to explain the frequent occurrence in patient sera of anti-Sm antibodies that cross-react with multiple Sm proteins and may ultimately further our understanding of how the snRNPs act as auto-antigens and immunogens in SLE.
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