ArticleJournal of molecular biology2008
Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals.
Article in Journal of molecular biology, 2008. 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, 34 citations in OpenAlex.
- Defenders of the Transcriptome: Guard Protein-Mediated mRNA Quality Control inInternational journal of molecular sciences · 2024Review
- RNA recognition by Npl3p reveals U2 snRNA-binding compatible with a chaperone role during splicing.Nature communications · 2023Article
- Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA.Nucleic acids research · 2023Article
- Parameterising Translational Feedback Models of Autoregulatory RNA-Binding Proteins inMicroorganisms · 2022Article
- The RNA binding protein Npl3 promotes resection of DNA double-strand breaks by regulating the levels of Exo1.Nucleic acids research · 2017Article
- Loss of the Yeast SR Protein Npl3 Alters Gene Expression Due to Transcription Readthrough.PLoS genetics · 2015Article
- Co-transcriptional mRNP formation is coordinated within a molecular mRNP packaging station in S. cerevisiae.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- Proteomic analyses reveal that Sky1 modulates apoptosis and mitophagy in Saccharomyces cerevisiae cells exposed to cisplatin.International journal of molecular sciences · 2014Article
- Npl3, a new link between RNA-binding proteins and the maintenance of genome integrity.Cell cycle (Georgetown, Tex.) · 2014Article
- Interactions affected by arginine methylation in the yeast protein-protein interaction network.Molecular & cellular proteomics : MCP · 2013Article
- Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Yeast hnRNP-related proteins contribute to the maintenance of telomeres.Biochemical and biophysical research communications · 2012Article
- The mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress.Molecular and cellular biology · 2010Article
- Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1.Journal of molecular biology · 2010Article
- Molecular mechanisms of eukaryotic pre-mRNA 3' end processing regulation.Nucleic acids research · 2010Review
- The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.Journal of molecular biology · 2009Article
- A single SR-like protein, Npl3, promotes pre-mRNA splicing in budding yeast.Molecular cell · 2008Article
- Physical protein-protein interactions predicted from microarrays.Bioinformatics (Oxford, England) · 2008Article
- Article
- Signals for pre-mRNA cleavage and polyadenylation.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Yeast Npl3 is homologous to SR proteins in higher eukaryotes, a family of RNA-binding proteins that have multiple essential roles in RNA metabolism. This protein competes with 3'-end processing factors for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. The NMR structure of its RNA-binding domain shows two unusually compact RNA recognition motifs (RRMs), and identifies the RNA recognition surface in Npl3. Biochemical and NMR studies identify a class of G+U-rich RNA sequences with high specificity for this protein. The protein binds to RNA and forms a single globular structure, but the two RRMs of Npl3 are not equivalent, with the second domain forming much stronger interactions with G+U-rich RNA sequences that occur independently of the interaction of the first RRM. The specific binding to G+U-rich RNAs observed for the two RRMs of Npl3 is masked in the full-length protein by a much stronger but non-sequence-specific RNA-binding activity residing outside of its RRMs. The preference of Npl3 for G+U-rich sequences supports the model for its function in regulating recognition of 3'-end processing sites through competition with the Rna15 (yeast analog of human CstF-64 protein) subunit of the processing complex.
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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.