ArticleJournal of molecular biology2011
Crystal structure of the plant epigenetic protein arginine methyltransferase 10.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- PRMT1 oligomerization regulates RNA-binding protein cascade to promote pancreatic cancer.Life science alliance · 2025Article
- OsPRMT6b balances plant growth and high temperature stress by feedback inhibition of abscisic acid signaling.Nature communications · 2025Article
- PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025Review
- R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment.International journal of molecular sciences · 2024Review
- Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity.Protein science : a publication of the Protein Society · 2024Article
- Naturally occurring cancer-associated mutations disrupt oligomerization and activity of protein arginine methyltransferase 1 (PRMT1).The Journal of biological chemistry · 2021Article
- Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.Cellular and molecular life sciences : CMLS · 2019Review
- Redox Control of Protein Arginine Methyltransferase 1 (PRMT1) Activity.The Journal of biological chemistry · 2015Article
- The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.Cellular and molecular life sciences : CMLS · 2015Review
- Computational Study of Symmetric Methylation on Histone Arginine Catalyzed by Protein Arginine Methyltransferase PRMT5 through QM/MM MD and Free Energy Simulations.Molecules (Basel, Switzerland) · 2015Article
- Functional interplay between protein arginine methyltransferases in Trypanosoma brucei.MicrobiologyOpen · 2014Article
- Article
- Cloning, expression, purification and preliminary X-ray crystallographic analysis of mouse protein arginine methyltransferase 7.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Control of histone H3 lysine 9 (H3K9) methylation state via cooperative two-step demethylation by Jumonji domain containing 1A (JMJD1A) homodimer.The Journal of biological chemistry · 2013Article
- Theoretical insights into catalytic mechanism of protein arginine methyltransferase 1.PloS one · 2013Article
- The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation.Protein & cell · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein arginine methyltransferase 10 (PRMT10) is a type I arginine methyltransferase that is essential for regulating flowering time in Arabidopsis thaliana. We present a 2.6 Å resolution crystal structure of A. thaliana PRMT 10 (AtPRMT10) in complex with a reaction product, S-adenosylhomocysteine. The structure reveals a dimerization arm that is 12-20 residues longer than PRMT structures elucidated previously; as a result, the essential AtPRMT10 dimer exhibits a large central cavity and a distinctly accessible active site. We employ molecular dynamics to examine how dimerization facilitates AtPRMT10 motions necessary for activity, and we show that these motions are conserved in other PRMT enzymes. Finally, functional data reveal that the 10 N-terminal residues of AtPRMT10 influence substrate specificity, and that enzyme activity is dependent on substrate protein sequences distal from the methylation site. Taken together, these data provide insights into the molecular mechanism of AtPRMT10, as well as other members of the PRMT family of enzymes. They highlight differences between AtPRMT10 and other PRMTs but also indicate that motions are a conserved element of PRMT function.
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