ArticleMolecular and cellular biology2012
The interaction of Prp2 with a defined region of the intron is required for the first splicing reaction.
Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 55 citations in OpenAlex.
- New mechanistic insights into Prp22-mediated exon ligation and mRNA release.Nucleic acids research · 2025Article
- Molecular basis for the activation of human spliceosome.Nature communications · 2024Article
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- Spliceosome assembly and regulation: insights from analysis of highly reduced spliceosomes.RNA (New York, N.Y.) · 2023Review
- Article
- Arresting Spliceosome Intermediates at Various Stages of the Splicing Pathway.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Overlapping roles of spliceosomal components SF3B1 and PHF5A in rice splicing regulation.Communications biology · 2021Article
- DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021Review
- Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Functional analysis of Cwc24 ZF-domain in 5' splice site selection.Nucleic acids research · 2019Article
- Structural Insights into Nuclear pre-mRNA Splicing in Higher Eukaryotes.Cold Spring Harbor perspectives in biology · 2019Review
- Dynamic protein-RNA interactions in mediating splicing catalysis.Nucleic acids research · 2019Article
- Molecular Mechanisms of pre-mRNA Splicing through Structural Biology of the Spliceosome.Cold Spring Harbor perspectives in biology · 2019Review
- Functional analysis of Hsh155/SF3b1 interactions with the U2 snRNA/branch site duplex.RNA (New York, N.Y.) · 2018Article
- Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018Article
- Cwc23 is a component of the NTR complex and functions to stabilize Ntr1 and facilitate disassembly of spliceosome intermediates.Nucleic acids research · 2018Article
- Yeast Prp2 liberates the 5' splice site and the branch site adenosine for catalysis of pre-mRNA splicing.RNA (New York, N.Y.) · 2017Article
- The RES complex is required for efficient transformation of the precatalytic B spliceosome into an activated BGenes & development · 2017Article
- Splicing and transcription touch base: co-transcriptional spliceosome assembly and function.Nature reviews. Molecular cell biology · 2017Review
- Methodologies for studying the spliceosome's RNA dynamics with single-molecule FRET.Methods (San Diego, Calif.) · 2017Review
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Saccharomyces cerevisiae, the 3' splice site is not required for the first catalytic reaction of splicing. We have previously reported that at least 24 nucleotides downstream of the branch point is required for the first reaction to take place, but the precatalytic spliceosome forms efficiently on the truncated pre-mRNA with only 5 nucleotides retained downstream of the branch point. The factors that mediate this length-dependent control of the first catalytic step are not known. We show here that Prp2 can be recruited to the spliceosome without interacting with pre-mRNA when the 3' tail is short. Prp2 interacts with the intron when the 3' tail is extended, which results in destabilization of Prp2 and, consequently, progression of the first reaction. An RNA segment at 23 to 33 nucleotides downstream of the branch point is necessary and sufficient for the ATP-dependent action of Prp2. We also show that Prp2 directly interacts with the carboxyl-terminal fragment of Brr2 by pulldown assays. We propose that Prp2 is recruited to the spliceosome via interaction with Brr2 and is spatially positioned to interact with this specific region of the pre-mRNA, which stimulates the ATPase activity of Prp2 to promote the progression of the first catalytic step.
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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.