ArticleNucleic acids research2017
A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Viral proteins suppress rice defenses by boosting OsTSN1 RNA decay via phase separation and multimerization.Nature communications · 2025Article
- Broad-spectrum resistance against multiple PVY-strains by CRSIPR/Cas13 system inGM crops & food · 2022Article
- Article
- Proteome expansion in the Potyviridae evolutionary radiation.FEMS microbiology reviews · 2022Review
- Argonaute 2 Controls Antiviral Activity against Sweet Potato Mild Mottle Virus inPlants (Basel, Switzerland) · 2021Article
- Multifaceted roles of RNA polymerase IV in plant growth and development.Journal of experimental botany · 2020Article
- RNA-induced initiation of transcriptional silencing (RITS) complex structure and function.RNA biology · 2019Review
- Generation of virus-resistant potato plants by RNA genome targeting.Plant biotechnology journal · 2019Article
- Antiviral ARGONAUTEs AgainstPlant physiology · 2019Article
- Review
- Antiviral Roles of Abscisic Acid in Plants.Frontiers in plant science · 2017Review
- Plant RNA Regulatory Network and RNA Granules in Virus Infection.Frontiers in plant science · 2017Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In most eukaryotes, RNA silencing is an adaptive immune system regulating key biological processes including antiviral defense. To evade this response, viruses of plants, worms and insects have evolved viral suppressors of RNA silencing proteins (VSRs). Various VSRs, such as P1 from Sweet potato mild mottle virus (SPMMV), inhibit the activity of RNA-induced silencing complexes (RISCs) including an ARGONAUTE (AGO) protein loaded with a small RNA. However, the specific mechanisms explaining this class of inhibition are unknown. Here, we show that SPMMV P1 interacts with AGO1 and AGO2 from Arabidopsis thaliana, but solely interferes with AGO1 function. Moreover, a mutational analysis of a newly identified zinc finger domain in P1 revealed that this domain could represent an effector domain as it is required for P1 suppressor activity but not for AGO1 binding. Finally, a comparative analysis of the target RNA binding capacity of AGO1 in the presence of wild-type or suppressor-defective P1 forms revealed that P1 blocks target RNA binding to AGO1. Our results describe the negative regulation of RISC, the small RNA containing molecular machine.
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Registered trials
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