ArticleRNA (New York, N.Y.)2006
Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 38 citations in OpenAlex.
- Manipulation of mitochondrial poly(A) polymerase family proteins inFrontiers in parasitology · 2023Article
- Arginine Methyltransferases as Regulators of RNA-Binding Protein Activities in Pathogenic Kinetoplastids.Frontiers in molecular biosciences · 2021Review
- Developmental regulation of edited CYb and COIII mitochondrial mRNAs is achieved by distinct mechanisms in Trypanosoma brucei.Nucleic acids research · 2020Article
- Cell-line specific RNA editing patterns in Trypanosoma brucei suggest a unique mechanism to generate protein variation in a system intolerant to genetic mutations.Nucleic acids research · 2020Article
- Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme).Journal of molecular biology · 2020Article
- Intrinsic and regulated properties of minimally edited trypanosome mRNAs.Nucleic acids research · 2019Article
- Article
- 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
- Global proteomic analysis in trypanosomes reveals unique proteins and conserved cellular processes impacted by arginine methylation.Journal of proteomics · 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
- Architecture of the trypanosome RNA editing accessory complex, MRB1.Nucleic acids research · 2012Article
- Protein arginine methylation in parasitic protozoa.Eukaryotic cell · 2011Review
- Structure of the Trypanosoma brucei p22 protein, a cytochrome oxidase subunit II-specific RNA-editing accessory factor.The Journal of biological chemistry · 2010Article
- Distinct and overlapping functions of MRP1/2 and RBP16 in mitochondrial RNA metabolism.Molecular and cellular biology · 2009Article
- Characterization of PRMT1 from Plasmodium falciparum.The Biochemical journal · 2009Article
- A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei.The Journal of biological chemistry · 2009Article
- The MRB1 complex functions in kinetoplastid RNA processing.RNA (New York, N.Y.) · 2009Article
- TbRGG2, an essential RNA editing accessory factor in two Trypanosoma brucei life cycle stages.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Arginine methylation is a post-translational modification that impacts gene expression in both the cytoplasm and nucleus. Here, we demonstrate that arginine methylation also affects mitochondrial gene expression in the protozoan parasite, Trypanosoma brucei. Down-regulation of the major trypanosome type I protein arginine methyltransferase, TbPRMT1, leads to destabilization of specific mitochondrial mRNAs. We provide evidence that some of these effects are mediated by the mitochondrial RNA-binding protein, RBP16, which we previously demonstrated affects both RNA editing and stability. TbPRMT1 catalyzes methylation of RBP16 in vitro. Further, MALDI-TOF-MS analysis of RBP16 isolated from TbPRMT1-depleted cells indicates that, in vivo, TbPRMT1 modifies two of the three known methylated arginine residues in RBP16. Expression of mutated, nonmethylatable RBP16 in T. brucei has a dominant negative effect, leading to destabilization of a subset of those mRNAs affected by TbPRMT1 depletion. Our results suggest that the specificity and multifunctional nature of RBP16 are due, at least in part, to the presence of differentially methylated forms of the protein. However, some effects of TbPRMT1 depletion on mitochondrial gene expression cannot be accounted for by RBP16 action. Thus, these data implicate additional, unknown methylproteins in mitochondrial gene regulation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.