ArticleRNA (New York, N.Y.)2004
Definition of a spliceosome interaction domain in yeast Prp2 ATPase.
Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026Review
- Molecular basis for the activation of human spliceosome.Nature communications · 2024Article
- Article
- The Terminal Extensions of Dbp7 Influence Growth and 60S Ribosomal Subunit Biogenesis inInternational journal of molecular sciences · 2023Article
- Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018Article
- Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways.RNA biology · 2016Article
- Insights into the activation of the helicase Prp43 by biochemical studies and structural mass spectrometry.Nucleic acids research · 2014Article
- RNA helicases in splicing.RNA biology · 2013Review
- The interaction of Prp2 with a defined region of the intron is required for the first splicing reaction.Molecular and cellular biology · 2012Article
- Functional roles of protein splicing factors.Bioscience reports · 2012Review
- Structural bioinformatics of the human spliceosomal proteome.Nucleic acids research · 2012Article
- Dynamics of the putative RNA helicase Spb4 during ribosome assembly in Saccharomyces cerevisiae.Molecular and cellular biology · 2011Article
- RNA-Seq analysis of splicing in Plasmodium falciparum uncovers new splice junctions, alternative splicing and splicing of antisense transcripts.Nucleic acids research · 2011Article
- Prp43p contains a processive helicase structural architecture with a specific regulatory domain.The EMBO journal · 2010Article
- Release of SF3 from the intron branchpoint activates the first step of pre-mRNA splicing.RNA (New York, N.Y.) · 2010Article
- Nucleomorph genome of Hemiselmis andersenii reveals complete intron loss and compaction as a driver of protein structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome.Genes & development · 2007Article
- Mutations in PRP43 that uncouple RNA-dependent NTPase activity and pre-mRNA splicing function.Biochemistry · 2006Article
- The splicing factor Prp43p, a DEAH box ATPase, functions in ribosome biogenesis.Molecular and cellular biology · 2006Article
- Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase that is critical for splicing.Molecular and cellular biology · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae splicing factor Prp2 is an RNA-dependent ATPase required before the first transesterification reaction in pre-mRNA splicing. Prp2 binds to the spliceosome in the absence of ATP and is released following ATP hydrolysis. It contains three domains: a unique N-terminal domain, a helicase domain that is highly conserved in the DExD/H protein family, and a C-terminal domain that is conserved in spliceosomal DEAH proteins Prp2, Prp16, Prp22, and Prp43. We examined the role of each domain of Prp2 by deletion mutagenesis. Whereas deletions of either the helicase or C-terminal domain are lethal, deletions in the N-terminal domain have no detectable effect on Prp2 activity. Overexpression of the C-terminal domain of Prp2 exacerbates the temperature-sensitive phenotype of a prp2(Ts) strain, suggesting that the C-domain interferes with the activity of the Prp2(Ts) protein. A genetic approach was then taken to study interactions between Prp2 and the spliceosome. Previously, we isolated dominant negative mutants in the helicase domain of Prp2 that inhibit the activity of wild-type Prp2 when the mutant protein is overexpressed. We mutagenized one prp2 release mutant gene and screened for loss of dominant negative function. Several weak binding mutants were isolated and mapped to the C terminus of Prp2, further indicating the importance of the C terminus in spliceosome binding. This study is the first to indicate that amino acid substitutions outside the helicase domain can abolish spliceosome contact and splicing activity of a spliceosomal DEAH protein.
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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.