ArticleNucleic acids research2019
The molecular mechanism of dsRNA processing by a bacterial Dicer.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Harnessing double-stranded RNA (dsRNA): a sustainable approach to pest management.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Review
- Characterization of dsRNA binding proteins through solubility analysis identifies ZNF385A as a dsRNA homeostasis regulator.Nature communications · 2025Article
- Revolutionizing immunization: a comprehensive review of mRNA vaccine technology and applications.Virology journal · 2025Review
- Current landscape of mRNA technologies and delivery systems for new modality therapeutics.Journal of biomedical science · 2024Review
- 5'-tRF-19-Q1Q89PJZ Suppresses the Proliferation and Metastasis of Pancreatic Cancer Cells via Regulating Hexokinase 1-Mediated Glycolysis.Biomolecules · 2023Article
- Dynamic Protein-RNA recognition in primary MicroRNA processing.Current opinion in structural biology · 2022Review
- Structural basis for Dicer-like function of an engineered RNase III variant and insights into the reaction trajectory of two-MgRNA biology · 2022Article
- RNase III, Ribosome Biogenesis and Beyond.Microorganisms · 2021Review
- Off-target effects of RNAi correlate with the mismatch rate between dsRNA and non-target mRNA.RNA biology · 2021Article
- Genetic Insight into the Domain Structure and Functions of Dicer-Type Ribonucleases.International journal of molecular sciences · 2021Review
- Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Members of the ribonuclease (RNase) III family regulate gene expression by processing dsRNAs. It was previously shown that Escherichia coli (Ec) RNase III recognizes dsRNA with little sequence specificity and the cleavage products are mainly 11 nucleotides (nt) long. It was also shown that the mutation of a glutamate (EcE38) to an alanine promotes generation of siRNA-like products typically 22 nt long. To fully characterize substrate specificity and product size of RNase IIIs, we performed in vitro cleavage of dsRNAs by Ec and Aquifex aeolicus (Aa) enzymes and delineated their products by next-generation sequencing. Surprisingly, we found that both enzymes cleave dsRNA at preferred sites, among which a guanine nucleotide was enriched at a specific position (+3G). Based on sequence and structure analyses, we conclude that RNase IIIs recognize +3G via a conserved glutamine (EcQ165/AaQ161) side chain. Abolishing this interaction by mutating the glutamine to an alanine eliminates the observed +3G preference. Furthermore, we identified a second glutamate (EcE65/AaE64), which, when mutated to alanine, also enhances the production of siRNA-like products. Based on these findings, we created a bacterial Dicer that is ideally suited for producing heterogeneous siRNA cocktails to be used in gene silencing studies.
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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.