ArticleNucleic acids research2017
The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Cell-type-specific ablation of siRNAs by Arabidopsis RTL1 reveals a role of phloem companion cells in systemic post-transcriptional gene silencing.Nucleic acids research · 2026Article
- Redox Regulation by Priming Agents Toward a Sustainable Agriculture.Plant & cell physiology · 2024Review
- Redox status of the plant cell determines epigenetic modifications under abiotic stress conditions and during developmental processes.Journal of advanced research · 2022Review
- Reactive oxygen species signalling in plant stress responses.Nature reviews. Molecular cell biology · 2022Review
- Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification.Metabolites · 2021Review
- Dicer-like proteins influence Arabidopsis root microbiota independent of RNA-directed DNA methylation.Microbiome · 2021Article
- Redox Components: Key Regulators of Epigenetic Modifications in Plants.International journal of molecular sciences · 2020Review
- Heat-Induced Oxidation of the Nuclei and Cytosol.Frontiers in plant science · 2020Article
- Thiol Based Redox Signaling in Plant Nucleus.Frontiers in plant science · 2018Review
Corrections and comments
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Authors and funding
14 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNase III enzymes cleave double stranded (ds)RNA. This is an essential step for regulating the processing of mRNA, rRNA, snoRNA and other small RNAs, including siRNA and miRNA. Arabidopsis thaliana encodes nine RNase III: four DICER-LIKE (DCL) and five RNASE THREE LIKE (RTL). To better understand the molecular functions of RNase III in plants we developed a biochemical assay using RTL1 as a model. We show that RTL1 does not degrade dsRNA randomly, but recognizes specific duplex sequences to direct accurate cleavage. Furthermore, we demonstrate that RNase III and dsRNA binding domains (dsRBD) are both required for dsRNA cleavage. Interestingly, the four DCL and the three RTL that carry dsRBD share a conserved cysteine (C230 in Arabidopsis RTL1) in their dsRBD. C230 is essential for RTL1 and DCL1 activities and is subjected to post-transcriptional modification. Indeed, under oxidizing conditions, glutathionylation of C230 inhibits RTL1 cleavage activity in a reversible manner involving glutaredoxins. We conclude that the redox state of the dsRBD ensures a fine-tune regulation of dsRNA processing by plant RNase III.
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Registered trials
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