ArticleThe Plant cell2022
Structure of plant RNA-DEPENDENT RNA POLYMERASE 2, an enzyme involved in small interfering RNA production.
Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- An evolutionarily conserved N-terminal domain of RRF-3 governs GTSF-1 binding in nematodes.EMBO reports · 2026Article
- Functional allelic diversity of PTGS components revealed by a high-throughput RUBY-based screening.The Plant journal : for cell and molecular biology · 2026Article
- RNA regulation in plants.Science China. Life sciences · 2026Review
- Epigenetics in the modern era of crop improvements.Science China. Life sciences · 2025Review
- Molecular Mechanisms Underlying the Establishment, Maintenance, and Removal of DNA Methylation in Plants.Annual review of plant biology · 2025Review
- DNA-dependent RNA polymerases in plants.The Plant cell · 2023Article
- Structure and mechanism of the plant RNA polymerase V.Science (New York, N.Y.) · 2023Article
- Enzymatic reactions of AGO4 in RNA-directed DNA methylation: siRNA duplex loading, passenger strand elimination, target RNA slicing, and sliced target retention.Genes & development · 2023Article
- Structural insights into the dual activities of the two-barrel RNA polymerase QDE-1.Nucleic acids research · 2022Article
- RDR2 in maize: one-way road to double-stranded RNA.The Plant cell · 2022Article
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7 authors at 3 institutions in 2 countries.
Funding
Abstract
In plants, the biogenesis of small interfering RNA (siRNA) requires a family of RNA-dependent RNA polymerases that convert single-stranded RNA (ssRNA) into double-stranded RNA (dsRNA), which is subsequently cleaved into defined lengths by Dicer endonucleases. Here, we determined the structure of maize (Zea mays) RNA-DEPENDENT RNA POLYMERASE 2 (ZmRDR2) in the closed and open conformations. The core catalytic region of ZmRDR2 possesses the canonical DNA-dependent RNA polymerase (DdRP) catalytic sites, pointing to a shared RNA production mechanism between DdRPs and plant RDR-family proteins. Apo-ZmRDR2 adopts a highly compact structure, representing an inactive closed conformation. By contrast, adding RNA induced a significant conformational change in the ZmRDR2 Head domain that opened the RNA binding tunnel, suggesting this is an active elongation conformation of ZmRDR2. Overall, our structural studies trapped both the active and inactive conformations of ZmRDR2, providing insights into the molecular mechanism of dsRNA synthesis during plant siRNA production.
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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.