ArticlePloS one2011
Characterization of the PRMT gene family in rice reveals conservation of arginine methylation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- Identification of candidate genes for watermelon (Molecular breeding : new strategies in plant improvement · 2025Article
- OsPRMT6b balances plant growth and high temperature stress by feedback inhibition of abscisic acid signaling.Nature communications · 2025Article
- A Brief Overview of the Epigenetic Regulatory Mechanisms in Plants.International journal of molecular sciences · 2025Review
- R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment.International journal of molecular sciences · 2024Review
- SISTER OF FCA physically associates with SKB1 to regulate flowering time in Arabidopsis thaliana.BMC plant biology · 2024Article
- Genome-wide identification and expression analysis of protein arginine methyltransferase and JmjC domain-containing family in apple.Frontiers in plant science · 2024Article
- Genome-Wide Identification of Maize Protein Arginine Methyltransferase Genes and Functional Analysis ofInternational journal of molecular sciences · 2022Article
- Dwarf and High Tillering1 represses rice tillering through mediating the splicing of D14 pre-mRNA.The Plant cell · 2022Article
- Genome-Wide Identification and Spatial Expression Analysis of Histone Modification Gene Families in the Rubber DandelionPlants (Basel, Switzerland) · 2022Article
- Comprehensive molecular evaluation of the histone methyltransferase gene family and their important roles in two-line hybrid wheat.BMC plant biology · 2022Article
- Article
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Genome-Wide Identification of Histone Modification Gene Families in the Model LegumePlants (Basel, Switzerland) · 2022Article
- Not all Is SET for Methylation: Evolution of Eukaryotic Protein Methyltransferases.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Molecular cloning and in-depth bioinformatics analysis of type II ribosome-inactivating protein isolated fromSaudi journal of biological sciences · 2020Article
- Global Proteomic Analysis Reveals Widespread Lysine Succinylation in Rice Seedlings.International journal of molecular sciences · 2019Article
- Protein arginine methyltransferases interact with intraflagellar transport particles and change location during flagellar growth and resorption.Molecular biology of the cell · 2017Article
- Root morphogenic pathways in Eucalyptus grandis are modified by the activity of protein arginine methyltransferases.BMC plant biology · 2017Article
- Correlations between predicted protein disorder and post-translational modifications in plants.Bioinformatics (Oxford, England) · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational methylation of arginine residues profoundly affects the structure and functions of protein and, hence, implicated in a myriad of essential cellular processes such as signal transduction, mRNA splicing and transcriptional regulation. Protein arginine methyltransferases (PRMTs), the enzymes catalyzing arginine methylation have been extensively studied in animals, yeast and, to some extent, in model plant Arabidopsis thaliana. Eight genes coding for the PRMTs were identified in Oryza sativa, previously. Here, we report that these genes show distinct expression patterns in various parts of the plant. In vivo targeting experiment demonstrated that GFP-tagged OsPRMT1, OsPRMT5 and OsPRMT10 were localized to both the cytoplasm and nucleus, whereas OsPRMT6a and OsPRMT6b were predominantly localized to the nucleus. OsPRMT1, OsPRMT4, OsPRMT5, OsPRMT6a, OsPRMT6b and OsPRMT10 exhibited in vitro arginine methyltransferase activity against myelin basic protein, glycine-arginine-rich domain of fibrillarin and calf thymus core histones. Furthermore, they depicted specificities for the arginine residues in histones H3 and H4 and were classified into type I and Type II PRMTs, based on the formation of type of dimethylarginine in the substrate proteins. The two homologs of OsPRMT6 showed direct interaction in vitro and further titrating different amounts of these proteins in the methyltransferase assay revealed that OsPRMT6a inhibits the methyltransferase activity of OsPRMT6b, probably, by the formation of heterodimer. The identification and characterization of PRMTs in rice suggests the conservation of arginine methylation in monocots and hold promise for gaining further insight into regulation of plant development.
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