ArticleJournal of biomedicine & biotechnology2009
Combined use of MS2 and PP7 coat fusions shows that TIA-1 dominates hnRNP A1 for K-SAM exon splicing control.
Article in Journal of biomedicine & biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Disordered C-terminal domain drives spatiotemporal confinement of RNAPII to enhance search for chromatin targets.Nature cell biology · 2024Article
- Disordered C-terminal domain drives spatiotemporal confinement of RNAPII to enhance search for chromatin targets.bioRxiv : the preprint server for biology · 2023Article
- HiFENS: high-throughput FISH detection of endogenous pre-mRNA splicing isoforms.Nucleic acids research · 2022Article
- hnRNP A1 in RNA metabolism regulation and as a potential therapeutic target.Frontiers in pharmacology · 2022Review
- Applications of phage-derived RNA-based technologies in synthetic biology.Synthetic and systems biotechnology · 2020Review
- Rational Design of Aptamer-Tagged tRNAs.International journal of molecular sciences · 2020Article
- PRC2 is dispensable forThe EMBO journal · 2017Article
- EMT and stemness: flexible processes tuned by alternative splicing in development and cancer progression.Molecular cancer · 2017Review
- hnRNP A1: the Swiss army knife of gene expression.International journal of molecular sciences · 2013Review
- Engineering naturally occurring trans-acting non-coding RNAs to sense molecular signals.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Splicing of the FGFR2 K-SAM exon is repressed by hnRNP A1 bound to the exon and activated by TIA-1 bound to the downstream intron. Both proteins are expressed similarly by cells whether they splice the exon or not, so it is important to know which one is dominant. To answer this question, we used bacteriophage PP7 and bacteriophage MS2 coat fusions to tether hnRNP A1 and TIA-1 to distinct sites on the same pre-mRNA molecule. hnRNP A1 fused to one coat protein was tethered to a K-SAM exon containing the corresponding coat protein's binding site. TIA-1 fused to the other coat protein was tethered to the downstream intron containing that coat protein's binding site. This led to efficient K-SAM exon splicing. Our results show that TIA-1 is dominant for K-SAM exon splicing control and validate the combined use of PP7 and MS2 coat proteins for studying posttranscriptional events.
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