ArticleCellular microbiology2012
PRMT1 methylates the single Argonaute of Toxoplasma gondii and is important for the recruitment of Tudor nuclease for target RNA cleavage by antisense guide RNA.
Article in Cellular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- In Vitro and In Silico Evaluation of the Anti-Infective Potential of EF24-Analogous Curcuminoids: Antiprotozoal Activity and HIV-1 Ribonuclease H Inhibition.Pathogens (Basel, Switzerland) · 2026Article
- Protein arginine methyltransferases in protozoan parasites: a new path for antiparasitic chemotherapy?Microbial cell (Graz, Austria) · 2026Article
- R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment.International journal of molecular sciences · 2024Review
- The unique dual targeting of AGO1 by two types of PRMT enzymes promotes phasiRNA loading in Arabidopsis thaliana.Nucleic acids research · 2024Article
- piRNA pathway evolution beyond gonad context: Perspectives from apicomplexa and trypanosomatids.Frontiers in genetics · 2023Article
- Bidirectional Functional Effects ofMicroorganisms · 2022Review
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Mutations in PpAGO3 Lead to Enhanced Virulence ofFrontiers in microbiology · 2022Article
- "Reading" a new chapter in protozoan parasite transcriptional regulation.PLoS pathogens · 2021Review
- Noncoding RNAs in Apicomplexan Parasites: An Update.Trends in parasitology · 2020Review
- Characterization of protein arginine methyltransferase of TgPRMT5 in Toxoplasma gondii.Parasites & vectors · 2019Article
- Tryptophan-kynurenine pathway attenuates β-catenin-dependent pro-parasitic role of STING-TICAM2-IRF3-IDO1 signalosome in Toxoplasma gondii infection.Cell death & disease · 2019Article
- Tudor staphylococcal nuclease is a structure-specific ribonuclease that degrades RNA at unstructured regions during microRNA decay.RNA (New York, N.Y.) · 2018Article
- Expansion and Divergence of Argonaute Genes in the Oomycete GenusFrontiers in microbiology · 2018Article
- The Tudor Staphylococcal Nuclease Protein ofFrontiers in cellular and infection microbiology · 2017Article
- Article
- Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone.Parasites & vectors · 2015Article
- Induction of interferon-stimulated genes by IRF3 promotes replication of Toxoplasma gondii.PLoS pathogens · 2015Article
- Transcript maturation in apicomplexan parasites.Current opinion in microbiology · 2014Review
- Genetic manipulation in Δku80 strains for functional genomic analysis of Toxoplasma gondii.Journal of visualized experiments : JoVE · 2013Article
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5 authors.
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Abstract
Argonaute (Ago) plays a central role in RNA interference in metazoans, but its status in lower organisms remains ill-defined. We report on the Ago complex of the unicellular protozoan, Toxoplasma gondii (Tg), an obligatory pathogen of mammalian hosts. The PIWI-like domain of TgAgo lacked the canonical DDE/H catalytic triad, explaining its weak target RNA cleavage activity. However, TgAgo associated with a stronger RNA slicer, a Tudor staphylococcal nuclease (TSN), and with a protein Arg methyl transferase, PRMT1. Mutational analysis suggested that the N-terminal RGG-repeat domain of TgAgo was methylated by PRMT1, correlating with the recruitment of TSN. The slicer activity of TgAgo was Mg(2+)-dependent and required perfect complementarity between the guide RNA and the target. In contrast, the TSN activity was Ca(2+) -dependent and required an imperfectly paired guide RNA. Ago knockout parasites showed essentially normal growth, but in contrast, the PRMT1 knockouts grew abnormally. Chemical inhibition of Arg-methylation also had an anti-parasitic effect. These results suggest that the parasitic PRMT1 plays multiple roles, and its loss affects the recruitment of a more potent second slicer to the parasitic RNA silencing complex, the exact mechanism of which remains to be determined.
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