ArticleRNA (New York, N.Y.)2016
A heterotrimer model of the complete Microprocessor complex revealed by single-molecule subunit counting.
Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 55 citations in OpenAlex.
- ERH promotes primary microRNA processing beyond cluster assistance.Nature communications · 2025Article
- MicroRNA MTCO3P38 Inhibits the TMOD1/MMP13 Pathway to Alleviate the Progression of Hepatocellular Carcinoma.Journal of Cancer · 2025Article
- FluoroTensor: Identification and tracking of colocalised molecules and their stoichiometries in multi-colour single molecule imaging via deep learning.Computational and structural biotechnology journal · 2024Article
- Combinatorial microRNA activity is essential for the transition of pluripotent cells from proliferation into dormancy.Genome research · 2024Article
- Review
- Regulatory role of RNA-binding proteins in microRNA biogenesis.Frontiers in molecular biosciences · 2024Review
- microRNAs in action: biogenesis, function and regulation.Nature reviews. Genetics · 2023Review
- Review
- Role of the proline-rich disordered domain of DROSHA in intronic microRNA processing.Genes & development · 2023Article
- Review
- MicroRNA biogenesis proteins follow tissue-dependent expression during freezing in Dryophytes versicolor.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2022Article
- Diffraction-Limited Molecular Cluster Quantification with Bayesian Nonparametrics.Nature computational science · 2022Article
- Elucidating the Role of Microprocessor Protein DGCR8 in Bending RNA Structures.Biophysical journal · 2020Article
- ERH facilitates microRNA maturation through the interaction with the N-terminus of DGCR8.Nucleic acids research · 2020Article
- Select amino acids in DGCR8 are essential for the UGU-pri-miRNA interaction and processing.Communications biology · 2020Article
- Mismatched and wobble base pairs govern primary microRNA processing by human Microprocessor.Nature communications · 2020Article
- The internal loops in the lower stem of primary microRNA transcripts facilitate single cleavage of human Microprocessor.Nucleic acids research · 2020Article
- Systems and Synthetic microRNA Biology: From Biogenesis to Disease Pathogenesis.International journal of molecular sciences · 2019Review
- The role of dietary phytochemicals in the carcinogenesis via the modulation of miRNA expression.Journal of cancer research and clinical oncology · 2019Review
- Dgcr8 knockout approaches to understand microRNA functions in vitro and in vivo.Cellular and molecular life sciences : CMLS · 2019Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
During microRNA (miRNA) biogenesis, the Microprocessor complex (MC), composed minimally of Drosha, an RNaseIII enzyme, and DGCR8, a double-stranded RNA-binding protein, cleaves the primary-miRNA (pri-miRNA) to release the pre-miRNA stem-loop structure. Size-exclusion chromatography of the MC, isolated from mammalian cells, suggested multiple copies of one or both proteins in the complex. However, the exact stoichiometry was unknown. Initial experiments suggested that DGCR8 bound pri-miRNA substrates specifically, and given that Drosha could not be bound or cross-linked to RNA, a sequential model for binding was established in which DGCR8 bound first and recruited Drosha. Therefore, many laboratories have studied DGCR8 binding to RNA in the absence of Drosha and have shown that deletion constructs of DGCR8 can multimerize in the presence of RNA. More recently, it was demonstrated that Drosha can bind pri-miRNA substrates in the absence of DGCR8, casting doubt on the sequential model of binding. In the same study, using a single-molecule photobleaching assay, fluorescent protein-tagged deletion constructs of DGCR8 and Drosha assembled into a heterotrimeric complex on RNA, comprising two DGCR8 molecules and one Drosha molecule. To determine the stoichiometry of Drosha and DGCR8 within the MC in the absence of added RNA, we also used a single-molecule photobleaching assay and confirmed the heterotrimeric model of the human MC. We demonstrate that a heterotrimeric complex is likely preformed in the absence of RNA and exists even when full-length proteins are expressed and purified from human cells, and when hAGT-derived tags are used rather than fluorescent proteins.
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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.