4YHV

Yeast Prp3 C-terminal fragment 325-469

Summary for 4YHV

• Entry DOI: 10.2210/pdb4yhv/pdb
• Related: 4YHU 4YHV 4YHW
• Descriptor: U4/U6 small nuclear ribonucleoprotein PRP3, ACETIC ACID (3 entities in total)
• Functional Keywords: spliceosomal protein, duf1115, rna-binding domain, ferredoxin-like fold, rna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus: Q03338
• Total number of polymer chains: 1
• Total formula weight: 17481.20

Authors

Liu, S.,Wahl, M.C. (deposition date: 2015-02-27, release date: 2015-07-22, Last modification date: 2024-01-10)

Primary citation

Liu, S.,Mozaffari-Jovin, S.,Wollenhaupt, J.,Santos, K.F.,Theuser, M.,Dunin-Horkawicz, S.,Fabrizio, P.,Bujnicki, J.M.,Luhrmann, R.,Wahl, M.C.
A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing.
Elife, 4:e07320-e07320, 2015

PubMed 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 reassembly after splicing.

PubMed: 26161500
DOI: 10.7554/eLife.07320

Experimental method

X-RAY DIFFRACTION (2 Å)