ArticleRNA (New York, N.Y.)2001
An in vitro-selected RNA-binding site for the KH domain protein PSI acts as a splicing inhibitor element.
Article in RNA (New York, N.Y.), 2001. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Insulin-like Growth Factor 2 mRNA-Binding Protein 2-a Potential Link Between Type 2 Diabetes Mellitus and Cancer.The Journal of clinical endocrinology and metabolism · 2021Review
- The Sex Determination Cascade in the Silkworm.Genes · 2021Review
- The Roles of Insulin-Like Growth Factor 2 mRNA-Binding Protein 2 in Cancer and Cancer Stem Cells.Stem cells international · 2018Review
- The PSI-U1 snRNP interaction regulates male mating behavior in Drosophila.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Biochemical identification of new proteins involved in splicing repression at the Drosophila P-element exonic splicing silencer.Genes & development · 2015Article
- P Transposable Elements in Drosophila and other Eukaryotic Organisms.Microbiology spectrum · 2015Review
- The Drosophila splicing factor PSI is phosphorylated by casein kinase II and tousled-like kinase.PloS one · 2013Article
- The N-terminus of FILIA forms an atypical KH domain with a unique extension involved in interaction with RNA.PloS one · 2012Article
- Identification and experimental validation of splicing regulatory elements in Drosophila melanogaster reveals functionally conserved splicing enhancers in metazoans.RNA (New York, N.Y.) · 2011Article
- Evolution of a tissue-specific splicing network.Genes & development · 2011Article
- Genome-wide analysis of alternative pre-mRNA splicing and RNA-binding specificities of the Drosophila hnRNP A/B family members.Molecular cell · 2009Article
- ZBP2 facilitates binding of ZBP1 to beta-actin mRNA during transcription.Molecular and cellular biology · 2007Article
- Distinct contributions of KH domains to substrate binding affinity of Drosophila P-element somatic inhibitor protein.RNA (New York, N.Y.) · 2006Article
- Fast-Find: a novel computational approach to analyzing combinatorial motifs.BMC bioinformatics · 2006Article
- Global analysis of positive and negative pre-mRNA splicing regulators in Drosophila.Genes & development · 2005Article
- Dichotomous splicing signals in exon flanks.Genome research · 2005Article
- Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes.Genes & development · 2005Article
- Determination and augmentation of RNA sequence specificity of the Nova K-homology domains.Nucleic acids research · 2004Article
- The KH-type RNA-binding protein PSI is required for Drosophila viability, male fertility, and cellular mRNA processing.Genes & development · 2002Article
- The KH domain facilitates the substrate specificity and unwinding processivity of DDX43 helicase.The Journal of biological chemistryArticle
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
P element somatic inhibitor (PSI) is a 97-kDa RNA-binding protein with four KH motifs that is involved in the inhibition of splicing of the Drosophila P element third intron (IVS3) in somatic cells. PSI interacts with a negative regulatory element in the IVS3 5' exon. This element contains two pseudo-5' splice sites, termed F1 and F2. To identify high affinity binding sites for the PSI protein, in vitro selection (SELEX) was performed using a random RNA oligonucleotide pool. Alignment of high affinity PSI-binding RNAs revealed a degenerate consensus sequence consisting of a short core motif of CUU flanked by alternative purines and pyrimidines. Interestingly, this sequence resembles the F2 pseudo-5' splice site in the P element negative regulatory element. Additionally, a negative in vitro selection of PCR-mutagenized P element 5' exon regulatory element RNAs identified two U residues in the F1 and F2 pseudo-5' splice sites as important nucleotides for PSI binding and the U residue in the F2 region is a nearly invariant nucleotide in the consensus SELEX motif. The high affinity PSI SELEX sequence acted as a splicing inhibitor when placed in the context of a P element splicing pre-mRNA in vitro. Data from in vitro splicing assays, UV crosslinking and RNA-binding competition experiments indicates a strong correlation between the binding affinities of PSI for the SELEX sequences and their ability to modulate splicing of P element IVS3 in vitro.
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