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  A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing.

Liu, S., Mozaffari-Jovin, S., Wollenhaupt, J., Santos, K. F., Theuser, M., Dunin-Horkawicz, S., et al. (2015). A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing. eLife, 4: e07320. doi:10.7554/eLife.07320.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-F4EF-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-1C46-F
Genre: Journal Article

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 Creators:
Liu, S.1, Author              
Mozaffari-Jovin, S.2, Author              
Wollenhaupt, J., Author
Santos, , K. F., Author
Theuser, M., Author
Dunin-Horkawicz, S., Author
Fabrizio, P.2, Author              
Bujnicki, J. M., Author
Lührmann, R.2, Author              
Wahl, M. C., Author
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1Research Group of X-Ray Crystallography, MPI for biophysical chemistry, Max Planck Society, ou_578578              
2Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              

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 Abstract: Prp3 is an essential U4/U6 di-snRNP-associated protein whose functions and molecular mechanisms in pre-mRNA splicing are presently poorly understood. We show by structural and biochemical analyses that Prp3 contains a bipartite U4/U6 di-snRNA-binding region comprising an expanded ferredoxin-like fold, which recognizes a 3'-overhang of U6 snRNA, and a preceding peptide, which binds U4/U6 stem II. Phylogenetic analyses revealed that the single-stranded RNA-binding domain is exclusively found in Prp3 orthologs, thus qualifying as a spliceosome-specific RNA interaction module. The composite double-stranded/single-stranded RNA-binding region assembles cooperatively with Snu13 and Prp31 on U4/U6 di-snRNAs and inhibits Brr2-mediated U4/U6 di-snRNA unwinding in vitro. RNP-disrupting mutations in Prp3 lead to U4/U6•U5 tri-snRNP assembly and splicing defects in vivo. Our results reveal how Prp3 acts as an important bridge between U4/U6 and U5 in the tri-snRNP and comparison with a Prp24-U6 snRNA recycling complex suggests how Prp3 may be involved in U4/U6 re-assembly after splicing.

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Language(s): eng - English
 Dates: 2015-07-10
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.07320
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Title: eLife
Source Genre: Journal
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Pages: 23 Volume / Issue: 4 Sequence Number: e07320 Start / End Page: - Identifier: -