ArticleCold Spring Harbor symposia on quantitative biology2019
Recognition of Poly(A) RNA through Its Intrinsic Helical Structure.
Article in Cold Spring Harbor symposia on quantitative biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Pontocerebellar hypoplasia linked mutations of the deadenylase Target of EGR1 (TOE1) impair thermal stability, ribonuclease activity, and oligomerization.The Journal of biological chemistry · 2026Article
- An A-rich linker between dengue virus tandem xrRNAs facilitates functional coordination.bioRxiv : the preprint server for biology · 2026Article
- Article
- Pentanucleotide guanine-rich WGGGW repeats, including CANVAS AGGGA repeats, form a variety of noncanonical structures.Nucleic acids research · 2026Article
- Biochemical characterizations of Pontocerebellar Hypoplasia linked mutations of Target of Egr1 (TOE1) reveal impacts on thermal stability, ribonuclease activity, and oligomerization.bioRxiv : the preprint server for biology · 2025Article
- Localized 2'-OH Acylation at Poly(A) Extends RNA Translation.Journal of the American Chemical Society · 2025Article
- Research progress of mRNA vaccines for infectious diseases.European journal of medical research · 2025Review
- Targeting Glioblastoma Stem Cells via EphA2: Structural Insights into the RNA Aptamer A40s for Precision Therapy.Journal of chemical information and modeling · 2025Article
- RNA folding kinetics control riboswitch sensitivity in vivo.Nature communications · 2025Article
- Stacking correlation length in single-stranded DNA.Nucleic acids research · 2024Article
- mRNA medicine: Recent progresses in chemical modification, design, and engineering.Nano research · 2024Article
- RNA tailing machinery drives amyloidogenic phase transition.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- RNA folding kinetics control riboswitch sensitivity in vivo.bioRxiv : the preprint server for biology · 2024Article
- The Battle for Survival: The Role of RNA Non-Canonical Tails in the Virus-Host Interaction.Metabolites · 2023Review
- Recent Advances and Innovations in the Preparation and Purification of In Vitro-Transcribed-mRNA-Based Molecules.Pharmaceutics · 2023Review
- Single-Molecular Dissection of Liquid-Liquid Phase Transitions.Journal of the American Chemical Society · 2023Article
- Recent Advances in Messenger Ribonucleic Acid (mRNA) Vaccines and Their Delivery Systems: A Review.Clinical pharmacology : advances and applications · 2023Review
- Thoughts on how to think (and talk) about RNA structure.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Advances in COVID-19 mRNA vaccine development.Signal transduction and targeted therapy · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The polyadenosine (poly(A)) tail, which is found on the 3' end of almost all eukaryotic messenger RNAs (mRNAs), plays an important role in the posttranscriptional regulation of gene expression. Shortening of the poly(A) tail, a process known as deadenylation, is thought to be the first and rate-limiting step of mRNA turnover. Deadenylation is performed by the Pan2-Pan3 and Ccr4-Not complexes that contain highly conserved exonuclease enzymes Pan2, and Ccr4 and Caf1, respectively. These complexes have been extensively studied, but the mechanisms of how the deadenylase enzymes recognize the poly(A) tail were poorly understood until recently. Here, we summarize recent work from our laboratory demonstrating that the highly conserved Pan2 exonuclease recognizes the poly(A) tail, not through adenine-specific functional groups, but through the conformation of poly(A) RNA. Our biochemical, biophysical, and structural investigations suggest that poly(A) forms an intrinsic base-stacked, single-stranded helical conformation that is recognized by Pan2, and that disruption of this structure inhibits both Pan2 and Caf1. This intrinsic structure has been shown to be important in poly(A) recognition in other biological processes, further underlining the importance of the unique conformation of poly(A).
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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.