title: RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.
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.
authors.affiliation: European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 102209, 69012 Heidelberg, Germany.
authors.forename: I
authors.initials: I
authors.lastname: Törö
authors.forename: S
authors.initials: S
authors.lastname: Thore
authors.forename: C
authors.initials: C
authors.lastname: Mayer
authors.forename: J
authors.initials: J
authors.lastname: Basquin
authors.forename: B
authors.initials: B
authors.lastname: Séraphin
authors.forename: D
authors.initials: D
authors.lastname: Suck
mesh_terms: D019843:Archaeal Proteins; D019611:Archaeoglobus fulgidus; D001483:Base Sequence; D001667:Binding, Competitive / Q000187:drug effects; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000378:metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009843:Oligoribonucleotides / Q000494:pharmacology; D011233:Precipitin Tests; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000502:physiology; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D016337:RNA, Catalytic / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D043262:Ribonuclease P; D017411:Ribonucleoproteins, Small Nuclear / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D017381:Spliceosomes / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D019843:Archaeal Proteins; D009843:Oligoribonucleotides; D016337:RNA, Catalytic; D016601:RNA-Binding Proteins; D017411:Ribonucleoproteins, Small Nuclear; C426828:Sm1 protein, Archaeoglobus fulgidus; C426829:Sm2 protein, Archaeoglobus fulgidus; D012313:RNA; D004722:Endoribonucleases; D043262:Ribonuclease P