ArticleProtein & cell2012
The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation.
Article in Protein & cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Research on the regulation mechanism of drought tolerance in wheat.Plant cell reports · 2025Review
- Role of methylation in vernalization and photoperiod pathway: a potential flowering regulator?Horticulture research · 2023Article
- Genome-wide identification of Brassicaceae histone modification genes and their responses to abiotic stresses in allotetraploid rapeseed.BMC plant biology · 2023Article
- Comprehensive molecular evaluation of the histone methyltransferase gene family and their important roles in two-line hybrid wheat.BMC plant biology · 2022Article
- 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
- A novel automethylation reaction in the Aspergillus nidulans LaeA protein generates S-methylmethionine.The Journal of biological chemistry · 2013Article
- NOT2 proteins promote polymerase II-dependent transcription and interact with multiple MicroRNA biogenesis factors in Arabidopsis.The Plant cell · 2013Article
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Authors and funding
5 authors.
Funding
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Abstract
Arabidopsis AtPRMT10 is a plant-specific type I protein arginine methyltransferase that can asymmetrically dimethylate arginine 3 of histone H4 with auto-methylation activity. Mutations of AtPRMT10 derepress FLOWERING LOCUS C (FLC) expression resulting in a late-flowering phenotype. Here, to further investigate the biochemical characteristics of AtPRMT10, we analyzed a series of mutated forms of the AtPRMT10 protein. We demonstrate that the conserved "VLD" residues and "double-E loop" are essential for enzymatic activity of AtPRMT10. In addition, we show that Arg54 and Cys259 of AtPRMT10, two residues unreported in animals, are also important for its enzymatic activity. We find that Arg13 of AtPRMT10 is the auto-methylation site. However, substitution of Arg13 to Lys13 does not affect its enzymatic activity. In vivo complementation assays reveal that plants expressing AtPRMT10 with VLD-AAA, E143Q or E152Q mutations retain high levels of FLC expression and fail to rescue the late-flowering phenotype of atprmt10 plants. Taken together, we conclude that the methyltransferase activity of AtPRMT10 is essential for repressing FLC expression and promoting flowering in Arabidopsis.
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