ArticleThe Biochemical journal2007
Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana.
Article in The Biochemical journal, 2007. 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, 43 citations in OpenAlex.
- Article
- CsPRMT5-mediated histone H4R3 dimethylation negatively regulates resistance to gray blight in tea plants (Horticulture research · 2025Article
- 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
- Interactions between metabolism and chromatin in plant models.Molecular metabolism · 2020Review
- Redox-Dependent Chromatin Remodeling: A New Function of Nitric Oxide as Architect of Chromatin Structure in Plants.Frontiers in plant science · 2019Review
- Papillae formation on trichome cell walls requires the function of the mediator complex subunit Med25.Plant molecular biology · 2017Article
- Root morphogenic pathways in Eucalyptus grandis are modified by the activity of protein arginine methyltransferases.BMC plant biology · 2017Article
- Evolution of disorder in Mediator complex and its functional relevance.Nucleic acids research · 2016Article
- Importance of Mediator complex in the regulation and integration of diverse signaling pathways in plants.Frontiers in plant science · 2015Review
- Arabidopsis protein arginine methyltransferase 3 is required for ribosome biogenesis by affecting precursor ribosomal RNA processing.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Correlations between predicted protein disorder and post-translational modifications in plants.Bioinformatics (Oxford, England) · 2014Article
- NOT2 proteins promote polymerase II-dependent transcription and interact with multiple MicroRNA biogenesis factors in Arabidopsis.The Plant cell · 2013Article
- Genome-wide analysis of histone modifiers in tomato: gaining an insight into their developmental roles.BMC genomics · 2013Article
- The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation.Protein & cell · 2012Article
- Dynamic regulation of H3K27 trimethylation during Arabidopsis differentiation.PLoS genetics · 2011Article
- Characterization of the PRMT gene family in rice reveals conservation of arginine methylation.PloS one · 2011Article
- Transgenerational inheritance and resetting of stress-induced loss of epigenetic gene silencing in Arabidopsis.Molecular plant · 2010Article
- Cooperation of multiple chromatin modifications can generate unanticipated stability of epigenetic States in Arabidopsis.The Plant cell · 2010Article
- Redundant requirement for a pair of PROTEIN ARGININE METHYLTRANSFERASE4 homologs for the proper regulation of Arabidopsis flowering time.Plant physiology · 2008Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arginine methylation of histone H3 and H4 plays important roles in transcriptional regulation in eukaryotes such as yeasts, fruitflies, nematode worms, fish and mammals; however, less is known in plants. In the present paper, we report the identification and characterization of two Arabidopsis thaliana protein arginine N-methyltransferases, AtPRMT1a and AtPRMT1b, which exhibit high homology with human PRMT1. Both AtPRMT1a and AtPRMT1b methylated histone H4, H2A, and myelin basic protein in vitro. Site-directed mutagenesis of the third arginine (R3) on the N-terminus of histone H4 to lysine (H4R3N) completely abolished the methylation of histone H4. When fused to GFP (green fluorescent protein), both methyltransferases localized to the cytoplasm as well as to the nucleus. Consistent with their subcellular distribution, GST (glutathione transferase) pull-down assays revealed an interaction between the two methyltransferases, suggesting that both proteins may act together in a functional unit. In addition, we demonstrated that AtFib2 (Arabidopsis thaliana fibrillarin 2), an RNA methyltransferase, is a potential substrate for AtPRMT1a and AtPRMT1b, and, furthermore, uncovered a direct interaction between the protein methyltransferase and the RNA methyltransferase. Taken together, our findings implicate AtPRMT1a and AtPRMT1b as H4-R3 protein arginine N-methyltransferases in Arabidopsis and may be involved in diverse biological processes inside and outside the nucleus.
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