ArticleCommunications biology2021
The conserved single-cleavage mechanism of animal DROSHA enzymes.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed, 11 citations in OpenAlex.
- Neuropathic Pain: Mapping the miRNA Landscape.Non-coding RNA · 2026Review
- Exosomal miRNAs and isomiRs: potential biomarkers for type 2 diabetes mellitus.Precision clinical medicine · 2024Review
- Non-canonical RNA substrates of Drosha lack many of the conserved features found in primary microRNA stem-loops.Scientific reports · 2024Article
- SRSF7 and SRSF3 depend on RNA sequencing motifs and secondary structures to regulate Microprocessor.Life science alliance · 2023Article
- Dissection of the Caenorhabditis elegans Microprocessor.Nucleic acids research · 2023Article
- Dynamic Protein-RNA recognition in primary MicroRNA processing.Current opinion in structural biology · 2022Review
- The Drosha-Independent MicroRNA6778-5p/GSK3Computational intelligence and neuroscience · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RNase III enzymes typically cleave both strands of double-stranded RNAs (dsRNAs). We recently discovered that a human RNase III, DROSHA, exhibits a single cleavage on the one strand of primary microRNAs (pri-miRNAs). This study revealed that DROSHAs from the other animals, including worms and flies, also show the single cleavage on dsRNAs. Furthermore, we demonstrated that the mechanism of single cleavage is conserved in animal DROSHA enzymes. In addition, the dsRNA-binding domain (dsRBD) and a 3p-strand cleavage-supporting helix (3pCSH) of the DROSHA enzymes foster a weak single cleavage on one strand, which ensures their double cleavages. Disrupting the interaction of dsRBD-RNA and 3pCSH-RNA by an internal loop (IL) and a 3pCSH-loop in the lower stem of pri-miRNAs, respectively, inhibits one of the double cleavages of DROSHAs, and this results in the single cleavage. Our findings expand our understanding of the enzymatic mechanisms of animal DROSHAs. They also indicate that there are currently unknown cellular functions of DROSHA enzymes using their single cleavage activity.
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Registered trials
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