ArticleJournal of molecular biology2007
Structure and interactions of the first three RNA recognition motifs of splicing factor prp24.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- Reviewing PTBP1 Domain Modularity in the Pre-Genomic Era: A Foundation to Guide the Next Generation of Exploring PTBP1 Structure-Function Relationships.International journal of molecular sciences · 2023Review
- Hinge like domain motion facilitates human RBMS1 protein binding to proto-oncogene c-myc promoter.Nucleic acids research · 2021Article
- RNA matchmaking in chromatin regulation.Biochemical Society transactions · 2020Review
- The life of U6 small nuclear RNA, from cradle to grave.RNA (New York, N.Y.) · 2018Review
- Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.RNA (New York, N.Y.) · 2017Article
- Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.RNA (New York, N.Y.) · 2016Review
- Structural requirements for protein-catalyzed annealing of U4 and U6 RNAs during di-snRNP assembly.Nucleic acids research · 2016Article
- A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins.Genes & development · 2014Article
- Core structure of the U6 small nuclear ribonucleoprotein at 1.7-Å resolution.Nature structural & molecular biology · 2014Article
- A molecular, phylogenetic and functional study of theOpen journal of animal sciences · 2013Article
- A phylogenetic study ofOpen journal of animal sciences · 2013Article
- Structural analyses of the pre-mRNA splicing machinery.Protein science : a publication of the Protein Society · 2013Review
- Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology.Journal of biomolecular NMR · 2013Article
- Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.Journal of molecular biology · 2012Article
- A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop.Nucleic acids research · 2011Article
- Apo raver1 structure reveals distinct RRM domain orientations.Protein science : a publication of the Protein Society · 2011Article
- Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24.RNA (New York, N.Y.) · 2010Article
- Interactions between PTB RRMs induce slow motions and increase RNA binding affinity.Journal of molecular biology · 2010Article
- (1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA.Biomolecular NMR assignments · 2009Article
- Structure of yeast U6 snRNPs: arrangement of Prp24p and the LSm complex as revealed by electron microscopy.RNA (New York, N.Y.) · 2008Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The essential Saccharomyces cerevisiae pre-messenger RNA splicing protein 24 (Prp24) has four RNA recognition motifs (RRMs) and facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 is a component of the free U6 small nuclear ribonucleoprotein particle (snRNP) but not the U4/U6 bi-snRNP, and so is thought to be displaced from U6 by U4/U6 base-pairing. The interaction partners of each of the four RRMs of Prp24 and how these interactions direct U4/U6 pairing are not known. Here we report the crystal structure of the first three RRMs and the solution structure of the first two RRMs of Prp24. Strikingly, RRM 2 forms extensive inter-domain contacts with RRMs 1 and 3. These contacts occupy much of the canonical RNA-binding faces (beta-sheets) of RRMs 1 and 2, but leave the beta-sheet of RRM 3 exposed. Previously identified substitutions in Prp24 that suppress mutations in U4 and U6 spliceosomal RNAs cluster primarily in the beta-sheet of RRM 3, but also in a conserved loop of RRM 2. RNA binding assays and chemical shift mapping indicate that a large basic patch evident on the surface of RRMs 1 and 2 is part of a high affinity U6 RNA binding site. Our results suggest that Prp24 binds free U6 RNA primarily with RRMs 1 and 2, which may remodel the U6 secondary structure. The beta-sheet of RRM 3 then influences U4/U6 pairing through interaction with an unidentified ligand.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.