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RNA binding in an Sm core domain: X‐ray structure and functional analysis of an archaeal Sm protein complex
Author(s) -
Törö Imre,
Thore Stéphane,
Mayer Claudine,
Basquin Jérôme,
Séraphin Bertrand,
Suck Dietrich
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.9.2293
Subject(s) - biology , rna , rna binding protein , protein structure , computational biology , genetics , biochemistry , gene
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.