ArticleEukaryotic cell2010
TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei.
Article in Eukaryotic cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Protein arginine methyltransferases in protozoan parasites: a new path for antiparasitic chemotherapy?Microbial cell (Graz, Austria) · 2026Article
- DRBD18 acts as a transcript-specific RNA editing auxiliary factor inRNA (New York, N.Y.) · 2025Article
- Manipulation of mitochondrial poly(A) polymerase family proteins inFrontiers in parasitology · 2023Article
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Arginine Methyltransferases as Regulators of RNA-Binding Protein Activities in Pathogenic Kinetoplastids.Frontiers in molecular biosciences · 2021Review
- Review
- PRMT6 Promotes Lung Tumor Progression via the Alternate Activation of Tumor-Associated Macrophages.Molecular cancer research : MCR · 2020Article
- Epigenetic Regulation of Transcription in Trypanosomatid Protozoa.Current genomics · 2018Review
- Genome-wide and protein kinase-focused RNAi screens reveal conserved and novel damage response pathways in Trypanosoma brucei.PLoS pathogens · 2017Article
- The Major Protein Arginine Methyltransferase inThe Journal of biological chemistry · 2017Article
- Intelligence: shared genetic basis between Mendelian disorders and a polygenic trait.European journal of human genetics : EJHG · 2015Article
- Arginine methylation of DRBD18 differentially impacts its opposing effects on the trypanosome transcriptome.Nucleic acids research · 2015Article
- Functional interplay between protein arginine methyltransferases in Trypanosoma brucei.MicrobiologyOpen · 2014Article
- Distinct roles of a mitogen-activated protein kinase in cytokinesis between different life cycle forms of Trypanosoma brucei.Eukaryotic cell · 2014Article
- Article
- New insights into the molecular mechanisms of mitosis and cytokinesis in trypanosomes.International review of cell and molecular biology · 2014Review
- Global proteomic analysis in trypanosomes reveals unique proteins and conserved cellular processes impacted by arginine methylation.Journal of proteomics · 2013Article
- A novel automethylation reaction in the Aspergillus nidulans LaeA protein generates S-methylmethionine.The Journal of biological chemistry · 2013Article
- Identification of a novel lipin homologue from the parasitic protozoan Trypanosoma brucei.BMC microbiology · 2013Article
- Proteomic analysis reveals diverse classes of arginine methylproteins in mitochondria of trypanosomes.Molecular & cellular proteomics : MCP · 2013Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). In Saccharomyces cerevisiae and mammals, this modification affects multiple cellular processes, such as chromatin remodeling leading to transcriptional regulation, RNA processing, DNA repair, and cell signaling. The protozoan parasite Trypanosoma brucei possesses five putative PRMTs in its genome. This is a large number of PRMTs relative to other unicellular eukaryotes, suggesting an important role for arginine methylation in trypanosomes. Here, we present the in vitro and in vivo characterization of a T. brucei enzyme homologous to human PRMT6, which we term TbPRMT6. Like human PRMT6, TbPRMT6 is a type I PRMT, catalyzing the production of monomethylarginine and asymmetric dimethylarginine residues. In in vitro methylation assays, TbPRMT6 utilizes bovine histones as a substrate, but it does not methylate several T. brucei glycine/arginine-rich proteins. As such, it exhibits a relatively narrow substrate specificity compared to other T. brucei PRMTs. Knockdown of TbPRMT6 in both procyclic form and bloodstream form T. brucei leads to a modest but reproducible effect on parasite growth in culture. Moreover, upon TbPRMT6 depletion, both PF and BF exhibit aberrant morphologies indicating defects in cell division, and these defects differ in the two life cycle stages. Mass spectrometry of TbPRMT6-associated proteins reveals histones, components of the nuclear pore complex, and flagellar proteins that may represent TbPRMT6 substrates contributing to the observed growth and morphological defects.
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