ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structural and biochemical insights into the dicing mechanism of mouse Dicer: a conserved lysine is critical for dsRNA cleavage.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 81 citations in OpenAlex.
- How Do DICER1 Syndrome Mutations Disrupt Catalysis? Unveiling Dicer Metal Binding Architecture and Mechanism of Action Using MD Simulations and QM/MM Calculations.Journal of computational chemistry · 2026Article
- Genome-wide identification, characterization and expression analysis of AGO, DCL, and RDR families in Chenopodium quinoa.Scientific reports · 2023Article
- Structural Insights into the Advances and Mechanistic Understanding of Human Dicer.Biochemistry · 2023Review
- A Structural View of miRNA Biogenesis and Function.Non-coding RNA · 2022Review
- Article
- Neovascular Macular Degeneration: A Review of Etiology, Risk Factors, and Recent Advances in Research and Therapy.International journal of molecular sciences · 2021Review
- A Glimpse of "Dicer Biology" Through the Structural and Functional Perspective.Frontiers in molecular biosciences · 2021Review
- Dicer up-regulation by inhibition of specific proteolysis in differentiating monocytic cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chronic Dicer1 deficiency promotes atrophic and neovascular outer retinal pathologies in mice.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.The EMBO journal · 2018Article
- The mutational landscape ofOncotarget · 2018Article
- Dicer uses distinct modules for recognizing dsRNA termini.Science (New York, N.Y.) · 2018Article
- The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.Nucleic acids research · 2017Article
- Overexpression and purification of Dicer and accessory proteins for biochemical and structural studies.Methods (San Diego, Calif.) · 2017Article
- Article
- Production of small RNAs by mammalian Dicer.Pflugers Archiv : European journal of physiology · 2016Review
- Article
- Induced folding in RNA recognition by Arabidopsis thaliana DCL1.Nucleic acids research · 2015Article
- From guide to target: molecular insights into eukaryotic RNA-interference machinery.Nature structural & molecular biology · 2015Review
- 'Black sheep' that don't leave the double-stranded RNA-binding domain fold.Trends in biochemical sciences · 2014Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Dicer, an RNase III enzyme, initiates RNA interference by processing precursor dsRNAs into mature microRNAs and small-interfering RNAs. It is also involved in loading and activation of the RNA-induced silencing complex. Here, we report the crystal structures of a catalytically active fragment of mouse Dicer, containing the RNase IIIb and dsRNA binding domains, in its apo and Cd(2+)-bound forms, at 1.68- and 2.8-A resolution, respectively. Models of this structure with dsRNA reveal that a lysine residue, highly conserved in Dicer RNase IIIa and IIIb domains and in Drosha RNase IIIb domains, has the potential to participate in the phosphodiester bond cleavage reaction by stabilizing the transition state and leaving group of the scissile bond. Mutational and enzymatic assays confirm the importance of this lysine in dsRNA cleavage, suggesting that this lysine represents a conserved catalytic residue of Dicers. The structures also reveals a approximately 45-aa region within the RNase IIIb domain that harbors an alpha-helix at the N-terminal half and a flexible loop at the C-terminal half, features not present in previously reported structures of homologous RNase III domains from either bacterial RNase III enzymes or Giardia Dicer. N-terminal residues of this alpha-helix have the potential to engage in minor groove interaction with dsRNA substrates.
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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.