Structural highlights
Function
[PRP24_YEAST] Binds preferentially to the U4/U6 hybrid snRNAs. Can stimulate the annealing of U4 and U6. Could participate in both the formation and disassembly of the U4/U6 hybrid during splicing.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 Apr;16(4):792-804. Epub 2010 Feb 24. PMID:20181740[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martin-Tumasz S, Reiter NJ, Brow DA, Butcher SE. Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24. RNA. 2010 Apr;16(4):792-804. Epub 2010 Feb 24. PMID:20181740 doi:10.1261/rna.1913310
