ArticleNature plants2024
RNA helicase Brr2a promotes miRNA biogenesis by properly remodelling secondary structure of pri-miRNAs.
Article in Nature plants, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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.
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Who cites it
6 citing papers in PubMed.
- The splicing factor BRR2a functions as a repressor of stress-inducible genes.Stress biology · 2026Article
- Unfolding of RNA secondary structure impairs RNA stability to fine-tune phosphate starvation responses in rice roots.Plant communications · 2026Article
- MicroRNAs in thyroid eye disease: expression signatures and clinical implications.Frontiers in immunology · 2026Review
- Advances in miRNA research: Unraveling the complexities of gene regulation.Animal models and experimental medicine · 2025Review
- Noncoding RNA-encoded peptides in cancer: biological functions, posttranslational modifications and therapeutic potential.Journal of hematology & oncology · 2025Review
- Addressing the tissue specificity of U5 snRNP spliceosomopathies.Frontiers in cell and developmental biology · 2025Article
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9 authors.
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Abstract
RNA secondary structure (RSS) of primary microRNAs (pri-miRNAs) is a key determinant for miRNA production. Here we report that RNA helicase (RH) Brr2a, best known as a spliceosome component, modulates the structural complexity of pri-miRNAs to fine tune miRNA yield. Brr2a interacts with microprocessor component HYL1 and its loss reduces the levels of miRNAs derived from both intron-containing and intron-lacking pri-miRNAs. Brr2a binds to pri-miRNAs in vivo and in vitro. Furthermore, Brr2a hydrolyses ATP and the activity can be significantly enhanced by pri-miRNAs. Consequently, Brr2a unwinds pri-miRNAs in vitro. Moreover, Brr2a variants with compromised ATPase or RH activity are incapable of unwinding pri-miRNA, and their transgenic plants fail to restore miRNA levels in brr2a-2. Importantly, most of tested pri-miRNAs display distinct RSS, rendering them unsuitable for efficient processing in brr2a mutants vs Col-0. Collectively, this study reveals that Brr2a plays a non-canonical role in miRNA production beyond splicing regulation.
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Registered trials
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