ArticleThe Journal of biological chemistry2014
A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Protein arginine methyltransferases in cardiovascular disease: mechanisms, therapeutic potential, and future directions.Frontiers in physiology · 2026Review
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Research progress on PRMTs involved in epigenetic modification and tumour signalling pathway regulation (Review).International journal of oncology · 2023Review
- Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023Review
- Naturally occurring cancer-associated mutations disrupt oligomerization and activity of protein arginine methyltransferase 1 (PRMT1).The Journal of biological chemistry · 2021Article
- Structure, Activity, and Function of PRMT1.Life (Basel, Switzerland) · 2021Review
- A Review of Specific Biomarkers of Chronic Renal Injury and Their Potential Application in Nonclinical Safety Assessment Studies.Toxicologic pathology · 2021Review
- Non-Histone Arginine Methylation by Protein Arginine Methyltransferases.Current protein & peptide science · 2020Review
- Recent advances in targeting protein arginine methyltransferase enzymes in cancer therapy.Expert opinion on therapeutic targets · 2018Review
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-site Architectures.The Journal of biological chemistry · 2016Article
- Protein Arginine Methylation and Citrullination in Epigenetic Regulation.ACS chemical biology · 2016Article
- Chemical biology of protein arginine modifications in epigenetic regulation.Chemical reviews · 2015Review
- The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.Cellular and molecular life sciences : CMLS · 2015Review
- Histone H2A and H4 N-terminal tails are positioned by the MEP50 WD repeat protein for efficient methylation by the PRMT5 arginine methyltransferase.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Protein arginine methylation is emerging as a significant post-translational modification involved in various cell processes and human diseases. As the major arginine methylation enzyme, protein arginine methyltransferase 1 (PRMT1) strictly generates monomethylarginine and asymmetric dimethylarginine (ADMA), but not symmetric dimethylarginine (SDMA). The two types of dimethylarginines can lead to distinct biological outputs, as highlighted in the PRMT-dependent epigenetic control of transcription. However, it remains unclear how PRMT1 product specificity is regulated. We discovered that a single amino acid mutation (Met-48 to Phe) in the PRMT1 active site enables PRMT1 to generate both ADMA and SDMA. Due to the limited amount of SDMA formed, we carried out quantum mechanical calculations to determine the free energies of activation of ADMA and SDMA synthesis. Our results indicate that the higher energy barrier of SDMA formation (ΔΔG(‡) = 3.2 kcal/mol as compared with ADMA) may explain the small amount of SDMA generated by M48F-PRMT1. Our study reveals unique energetic challenges for SDMA-forming methyltransferases and highlights the exquisite control of product formation by active site residues in the PRMTs.
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Registered trials
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