ArticleThe Journal of biological chemistry2010
Double-stranded RNA-dependent ATPase DRH-3: insight into its role in RNAsilencing in Caenorhabditis elegans.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 34 citations in OpenAlex.
- An evolutionarily conserved N-terminal domain of RRF-3 governs GTSF-1 binding in nematodes.EMBO reports · 2026Article
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- Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance.Protein science : a publication of the Protein Society · 2024Article
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- The molecular mechanism of RIG-I activation and signaling.Immunological reviews · 2021Review
- Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3).Nucleic acids research · 2021Article
- Functional Characterization of the Cnidarian Antiviral Immune Response Reveals Ancestral Complexity.Molecular biology and evolution · 2021Article
- Article
- Parts, assembly and operation of the RIG-I family of motors.Current opinion in structural biology · 2014Review
- Dicer-related helicase 3 forms an obligate dimer for recognizing 22G-RNA.Nucleic acids research · 2014Article
- Duplex RNA activated ATPases (DRAs): platforms for RNA sensing, signaling and processing.RNA biology · 2013Review
- Article
- Phosphate and R2D2 restrict the substrate specificity of Dicer-2, an ATP-driven ribonuclease.Molecular cell · 2011Article
- Short double-stranded RNAs with an overhanging 5' ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
RNA helicases are proteins essential to almost every facet of RNA metabolism, including the gene-silencing pathways that employ small RNAs. A phylogenetically related group of helicases is required for the RNA-silencing mechanism in Caenorhabditis elegans. Dicer-related helicase 3 (DRH-3) is a Dicer-RIG-I family protein that is essential for RNA silencing and germline development in nematodes. Here we performed a biochemical characterization of the ligand binding and catalytic activities of DRH-3 in vitro. We identify signature motifs specific to this family of RNA helicases. We find that DRH-3 binds both single-stranded and double-stranded RNAs with high affinity. However, the ATPase activity of DRH-3 is stimulated only by double-stranded RNA. DRH-3 is a robust RNA-stimulated ATPase with a k(cat) value of 500/min when stimulated with short RNA duplexes. The DRH-3 ATPase may have allosteric regulation in cis that is controlled by the stoichiometry of double-stranded RNA to enzyme. We observe that the DRH-3 ATPase is stimulated only by duplexes containing RNA, suggesting a role for DRH-3 during or after transcription. Our findings provide clues to the role of DRH-3 during the RNA interference response in vivo.
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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.