ArticleThe EMBO journal2001
RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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79 citing papers in PubMed, 170 citations in OpenAlex.
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- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- The yxiD gene from Bacillus subtilis 6633 encodes a polymorphic toxin with tRNase activity and is neutralized by the cognate immunity protein YxxD.Nucleic acids research · 2025Article
- Interconversion and mechanisms between Lsm-type and Sm-type heteroheptameric rings: implications for spliceosome evolution and RNA metabolism.Nucleic acids research · 2025Article
- An ancestral fold reveals the evolutionary link between RNA polymerase and ribosomal proteins.Nature communications · 2024Article
- Analysis of Lsm Protein-Mediated Regulation in the HaloarchaeonInternational journal of molecular sciences · 2024Article
- The splicing factor SNRPB promotes ovarian cancer progression through regulating aberrant exon skipping of POLA1 and BRCA2.Oncogene · 2023Article
- Comprehensive Bioinformatics Analysis of the Biodiversity of Lsm Proteins in theMicroorganisms · 2023Article
- Alternative Splicing in the Regulatory Circuit of Plant Temperature Response.International journal of molecular sciences · 2023Review
- Tandem repeats in giant archaeal Borg elements undergo rapid evolution and create new intrinsically disordered regions in proteins.PLoS biology · 2023Article
- The Sm core components of small nuclear ribonucleoproteins promote homologous recombination repair.DNA repair · 2021Article
- The ChloroplastCells · 2021Review
- Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites.Nucleic acids research · 2020Article
- Article
- A regulatory RNA is involved in RNA duplex formation and biofilm regulation in Sulfolobus acidocaldarius.Nucleic acids research · 2018Article
- The SmAP2 RNA binding motif in the 3'UTR affects mRNA stability in the crenarchaeum Sulfolobus solfataricus.Nucleic acids research · 2017Article
- The SmAP1/2 proteins of the crenarchaeon Sulfolobus solfataricus interact with the exosome and stimulate A-rich tailing of transcripts.Nucleic acids research · 2017Article
- Re-refinement of the spliceosomal U4 snRNP core-domain structure.Acta crystallographica. Section D, Structural biology · 2016Article
- The Heptameric SmAP1 and SmAP2 Proteins of the Crenarchaeon Sulfolobus Solfataricus Bind to Common and Distinct RNA Targets.Life (Basel, Switzerland) · 2015Article
- Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes.RNA (New York, N.Y.) · 2014Article
19 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic Sm and Sm-like proteins associate with RNA to form the core domain of ribonucleoprotein particles involved in pre-mRNA splicing and other processes. Recently, putative Sm proteins of unknown function have been identified in Archaea. We show by immunoprecipitation experiments that the two Sm proteins present in Archaeoglobus fulgidus (AF-Sm1 and AF-Sm2) associate with RNase P RNA in vivo, suggesting a role in tRNA processing. The AF-Sm1 protein also interacts specifically with oligouridylate in vitro. We have solved the crystal structures of this protein and a complex with RNA. AF-Sm1 forms a seven-membered ring, with the RNA interacting inside the central cavity on one face of the doughnut-shaped complex. The bases are bound via stacking and specific hydrogen bonding contacts in pockets lined by residues highly conserved in archaeal and eukaryotic Sm proteins, while the phosphates remain solvent accessible. A comparison with the structures of human Sm protein dimers reveals closely related monomer folds and intersubunit contacts, indicating that the architecture of the Sm core domain and RNA binding have been conserved during evolution.
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