ArticleThe Journal of biological chemistry2014
Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.
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 30 papers.
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Who cites it
30 citing papers in PubMed, 60 citations in OpenAlex.
- Protein arginine methyltransferase 7-mediated arginine mono-methylation stabilizes SRY-box transcription factor 9 to promote non-small cell lung cancer progression.Molecular biomedicine · 2025Article
- Protein arginine methyltransferase 7 regulates the cell cycle and promotes the progression of prostate cancer.Oncology letters · 2025Article
- Mechanistic Insights into SAM-Dependent Methyltransferases: A Review of Computational Approaches.International journal of molecular sciences · 2025Review
- PRMT7-Mediated PTEN Activation Enhances Bone Regeneration in Female Mice.International journal of molecular sciences · 2025Article
- PRMT-7/PRMT7 activates HLH-30/TFEB to guard plasma membrane integrity compromised by bacterial pore-forming toxins.Autophagy · 2024Article
- Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor.Journal of medicinal chemistry · 2023Article
- Chemical probes and methods for the study of protein arginine methylation.RSC chemical biology · 2023Review
- Arginine Methylation of the PGC-1α C-Terminus Is Temperature-Dependent.Biochemistry · 2023Article
- The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.PloS one · 2023Article
- Systematic histone H4 replacement in Arabidopsis thaliana reveals a role for H4R17 in regulating flowering time.The Plant cell · 2022Article
- An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression.Nature communications · 2022Article
- Discovery of a potent and dual-selective bisubstrate inhibitor for protein arginine methyltransferase 4/5.Acta pharmaceutica Sinica. B · 2021Article
- Structure and Function of Protein Arginine Methyltransferase PRMT7.Life (Basel, Switzerland) · 2021Review
- Chemoproteomic Study Uncovers HemK2/KMT9 As a New Target for NTMT1 Bisubstrate Inhibitors.ACS chemical biology · 2021Article
- Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.Nature communications · 2021Article
- Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.Nature communications · 2020Article
- PRMT5 in gene regulation and hematologic malignancies.Genes & diseases · 2019Review
- Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.Cellular and molecular life sciences : CMLS · 2019Review
- The Biological Axis of Protein Arginine Methylation and Asymmetric Dimethylarginine.International journal of molecular sciences · 2019Review
- PRMT7 as a unique member of the protein arginine methyltransferase family: A review.Archives of biochemistry and biophysics · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein arginine methyltransferase 7 (PRMT7) methylates arginine residues on various protein substrates and is involved in DNA transcription, RNA splicing, DNA repair, cell differentiation, and metastasis. The substrate sequences it recognizes in vivo and the enzymatic mechanism behind it, however, remain to be explored. Here we characterize methylation catalyzed by a bacterially expressed GST-tagged human PRMT7 fusion protein with a broad range of peptide and protein substrates. After confirming its type III activity generating only ω-N(G)-monomethylarginine and its distinct substrate specificity for RXR motifs surrounded by basic residues, we performed site-directed mutagenesis studies on this enzyme, revealing that two acidic residues within the double E loop, Asp-147 and Glu-149, modulate the substrate preference. Furthermore, altering a single acidic residue, Glu-478, on the C-terminal domain to glutamine nearly abolished the activity of the enzyme. Additionally, we demonstrate that PRMT7 has unusual temperature dependence and salt tolerance. These results provide a biochemical foundation to understanding the broad biological functions of PRMT7 in health and disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.