ArticleRNA (New York, N.Y.)2019
Biophysical characterizations of the recognition of the AAUAAA polyadenylation signal.
Article in RNA (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- Poly(A) tail regulation in stem cells and early development.Cell regeneration (London, England) · 2025Review
- Molecular basis for the recognition of low-frequency polyadenylation signals by mPSF.Nucleic acids research · 2025Article
- SINE retrotransposons import polyadenylation signals to 3'UTRs in dog (Canis familiaris).Mobile DNA · 2025Article
- Quantifying negative selection in human 3' UTRs uncovers constrained targets of RNA-binding proteins.Nature communications · 2024Article
- 3'-End Processing of Eukaryotic mRNA: Machinery, Regulation, and Impact on Gene Expression.Annual review of biochemistry · 2023Review
- Human histone pre-mRNA assembles histone or canonical mRNA-processing complexes by overlapping 3'-end sequence elements.Nucleic acids research · 2022Article
- Molecular basis for the recognition of the AUUAAA polyadenylation signal by mPSF.RNA (New York, N.Y.) · 2022Article
- Molecular Insights into mRNA Polyadenylation and Deadenylation.International journal of molecular sciences · 2022Review
- RBBP6 activates the pre-mRNA 3' end processing machinery in humans.Genes & development · 2022Article
- Analysis Polyadenylation Signal Usage inAnimals : an open access journal from MDPI · 2022Article
- Enhanced Transgene Expression by Optimization of Poly A in Transfected CHO Cells.Frontiers in bioengineering and biotechnology · 2022Article
- Article
- Understanding RNA Binding by the Nonclassical Zinc Finger Protein CPSF30, a Key Factor in Polyadenylation during Pre-mRNA Processing.Biochemistry · 2021Article
- Molecular mechanism for the interaction between human CPSF30 and hFip1.Genes & development · 2020Article
- Recent molecular insights into canonical pre-mRNA 3'-end processing.Transcription · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Most eukaryotic messenger RNA precursors must undergo 3'-end cleavage and polyadenylation for maturation. We and others recently reported the structure of the AAUAAA polyadenylation signal (PAS) in complex with the protein factors CPSF-30, WDR33, and CPSF-160, revealing the molecular mechanism for this recognition. Here we have characterized in detail the interactions between the PAS RNA and the protein factors using fluorescence polarization experiments. Our studies show that AAUAAA is recognized with ∼3 nM affinity by the CPSF-160-WDR33-CPSF-30 ternary complex. Variations in the RNA sequence can greatly reduce the affinity. Similarly, mutations of CPSF-30 residues that have van der Waals interactions with the bases of AAUAAA also lead to substantial reductions in affinity. Finally, our studies confirm that both CPSF-30 and WDR33 are required for high-affinity binding of the PAS RNA, while these two proteins alone and their binary complexes with CPSF-160 have much lower affinity for the RNA.
Indexed as
Identifiers
What OpenQuestion holds
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.