ArticleGenes & development2007
The Prp18 protein stabilizes the interaction of both exons with the U5 snRNA during the second step of pre-mRNA splicing.
Article in Genes & development, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 45 citations in OpenAlex.
- A non-catalytic interaction surface mediates recognition of spliceosomal factors by the Toxoplasma gondii cyclophilin TgCyp23.The Biochemical journal · 2026Article
- Article
- Control of 3' splice site selection by the yeast splicing factor Fyv6.bioRxiv : the preprint server for biology · 2024Article
- Splicing factor Prp18p promotes genome-wide fidelity of consensus 3'-splice sites.Nucleic acids research · 2023Article
- Biochemical and genetic evidence supports Fyv6 as a second-step splicing factor inRNA (New York, N.Y.) · 2023Article
- The Arabidopsis cyclophilin CYP18-1 facilitates PRP18 dephosphorylation and the splicing of introns retained under heat stress.The Plant cell · 2022Article
- Tsukushi proteoglycan maintains RNA splicing and developmental signaling network in GFAP-expressing subventricular zone neural stem/progenitor cells.Frontiers in cell and developmental biology · 2022Article
- Genome-wide analysis of CCHC-type zinc finger (ZCCHC) proteins in yeast, Arabidopsis, and humans.Cellular and molecular life sciences : CMLS · 2020Review
- A Collection of Pre-mRNA Splicing Mutants inG3 (Bethesda, Md.) · 2020Article
- PRP4KA, a Putative Spliceosomal Protein Kinase, Is Important for Alternative Splicing and Development inGenetics · 2018Article
- A Genetic Screen Identifies PRP18a, a Putative Second Step Splicing Factor Important for Alternative Splicing and a Normal Phenotype inG3 (Bethesda, Md.) · 2018Article
- Postcatalytic spliceosome structure reveals mechanism of 3'-splice site selection.Science (New York, N.Y.) · 2017Article
- The Fission Yeast Pre-mRNA-processing Factor 18 (prp18+) Has Intron-specific Splicing Functions with Links to G1-S Cell Cycle Progression.The Journal of biological chemistry · 2016Article
- Prp8 retinitis pigmentosa mutants cause defects in the transition between the catalytic steps of splicing.RNA (New York, N.Y.) · 2016Article
- Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast.Molecular biology of the cell · 2016Article
- Cwc21p promotes the second step conformation of the spliceosome and modulates 3' splice site selection.Nucleic acids research · 2015Article
- Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system.RNA (New York, N.Y.) · 2013Article
- Brr2p-mediated conformational rearrangements in the spliceosome during activation and substrate repositioning.Genes & development · 2012Article
- Functional roles of protein splicing factors.Bioscience reports · 2012Review
- Spliceosome structure and function.Cold Spring Harbor perspectives in biology · 2011Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Interaction of the ends of the exons with loop 1 of the U5 snRNA aligns the exons for ligation in the second step of pre-mRNA splicing. To study the effect of Prp18 on the exons' interactions, we analyzed the splicing of pre-mRNAs with random sequences in the exon bases at the splice junctions. The exon mutations had large effects on splicing in yeast with a Prp18 protein lacking its most conserved region, but not in wild-type yeast. Analysis of splicing kinetics demonstrated that only the second step was affected in vivo and in vitro, showing that Prp18 - and specifically its conserved region - plays a key role in stabilizing the interaction of the exons with the spliceosome at the time of exon joining. Superior exon sequences defined by the prp18 results accelerated the second step of splicing by wild-type spliceosomes with inefficient AT-AC pre-mRNAs, implying that normal exon interactions follow the rules we discerned for prp18 splicing. Our results show that As are preferred at the ends of both exons and support a revised model of the interactions of the exons with U5 in which the exons are arranged in a continuous double helix that facilitates the second reaction.
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Registered trials
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.