Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24.

Martin-Tumasz S, Reiter NJ, Brow DA, Butcher SE
RNA. 2010 16 (4): 792-804

PMID: 20181740 · PMCID: PMC2844626 · DOI:10.1261/rna.1913310

U6 RNA plays a critical role in pre-mRNA splicing. Assembly of U6 into the spliceosome requires a significant structural rearrangement and base-pairing with U4 RNA. In the yeast Saccharomyces cerevisiae, this process requires the essential splicing factor Prp24. We present the characterization and structure of a complex containing one of Prp24's four RNA recognition motif (RRM) domains, RRM2, and a fragment of U6 RNA. NMR methods were used to identify the preferred U6 binding sequence of RRM2 (5'-GAGA-3'), measure the affinity of the interaction, and solve the structure of RRM2 bound to the hexaribonucleotide AGAGAU. Interdomain contacts observed between RRM2 and RRM3 in a crystal structure of the free protein are not detectable in solution. A structural model of RRM1 and RRM2 bound to a longer segment of U6 RNA is presented, and a partial mechanism for Prp24's annealing activity is proposed.

MeSH Terms (14)

Base Sequence Binding Sites Conserved Sequence DNA Helicases Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Structure, Tertiary Ribonucleoproteins, Small Nuclear Ribonucleoside Diphosphate Reductase RNA, Fungal RNA, Small Nuclear Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins

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