ArticleThe Journal of biological chemistry2009
A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 55 citations in OpenAlex.
- Protein arginine methyltransferases as metabolic regulators: many roles beyond cancer.Science China. Life sciences · 2026Review
- Protein arginine methyltransferase 7 regulates the cell cycle and promotes the progression of prostate cancer.Oncology letters · 2025Article
- Mechanistic Insights into SAM-Dependent Methyltransferases: A Review of Computational Approaches.International journal of molecular sciences · 2025Review
- DRBD18 acts as a transcript-specific RNA editing auxiliary factor inRNA (New York, N.Y.) · 2025Article
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Article
- The Effects of Flavonoid Apigenin on Male Reproductive Health: Inhibition of Spermatogonial Proliferation through Downregulation ofInternational journal of molecular sciences · 2021Article
- Structure and Function of Protein Arginine Methyltransferase PRMT7.Life (Basel, Switzerland) · 2021Review
- Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.Nature communications · 2021Article
- Arginine Methyltransferases as Regulators of RNA-Binding Protein Activities in Pathogenic Kinetoplastids.Frontiers in molecular biosciences · 2021Review
- PRMT7 regulates RNA-binding capacity and protein stability in Leishmania parasites.Nucleic acids research · 2020Article
- PRMT7 as a unique member of the protein arginine methyltransferase family: A review.Archives of biochemistry and biophysics · 2019Review
- Epigenetic Regulation of Transcription in Trypanosomatid Protozoa.Current genomics · 2018Review
- Caenorhabditis elegans PRMT-7 and PRMT-9 Are Evolutionarily Conserved Protein Arginine Methyltransferases with Distinct Substrate Specificities.Biochemistry · 2017Article
- Comparative Monomethylarginine Proteomics Suggests that Protein Arginine Methyltransferase 1 (PRMT1) is a Significant Contributor to Arginine Monomethylation inMolecular & cellular proteomics : MCP · 2017Article
- The Major Protein Arginine Methyltransferase inThe Journal of biological chemistry · 2017Article
- Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-site Architectures.The Journal of biological chemistry · 2016Article
- A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.Nucleic acids research · 2015Article
- Arginine methylation of DRBD18 differentially impacts its opposing effects on the trypanosome transcriptome.Nucleic acids research · 2015Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Arginine methylation is a widespread post-translational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). The ancient protozoan parasite, Trypanosoma brucei, possesses five putative PRMTs, a relatively large number for a single-celled eukaryote. Trypanosomatids lack gene regulation at the level of transcription, instead relying on post-transcriptional control mechanisms that act at the levels of RNA turnover, translation, and editing, all processes that likely involve multiple RNA-binding proteins, which are common targets of arginine methylation. Here, we report the characterization of a trypanosome PRMT, TbPRMT7, which is homologous to human PRMT7. Interestingly, trypanosomatids are the only single-celled eukaryotes known to harbor a PRMT7 homologue. TbPRMT7 differs dramatically from all known metazoan PRMT7 homologues in lacking the second AdoMet binding-like domain that is required for activity of the human enzyme. Nevertheless, bacterially expressed TbPRMT7 exhibits robust methyltransferase activity toward multiple targets in vitro. High resolution ion exchange chromatography analysis of methylated substrates reveals that TbPRMT7 is a type III PRMT, catalyzing the formation of only monomethylarginine, thereby representing the only exclusively type III PRMT identified to date. TbPRMT7 is expressed in both mammalian and insect stage T. brucei and is apparently dispensable for growth in both life cycle stages. The enzyme is cytoplasmically localized and is a component of several higher order complexes in vivo. Together, our studies indicate that TbPRMT7 is a Type III PRMT, and its robust activity and presence in numerous complexes suggest it plays multiple roles during the complex T. brucei life cycle.
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