ArticleBiochemistry2015
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- PRMT1 oligomerization regulates RNA-binding protein cascade to promote pancreatic cancer.Life science alliance · 2025Article
- CsPRMT5-mediated histone H4R3 dimethylation negatively regulates resistance to gray blight in tea plants (Horticulture research · 2025Article
- PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025Review
- Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity.Protein science : a publication of the Protein Society · 2024Article
- Dysregulation of arginine methylation in tumorigenesis.Frontiers in molecular biosciences · 2024Review
- The Role of Protein Arginine Methyltransferases in DNA Damage Response.International journal of molecular sciences · 2022Review
- Activity and Function of the PRMT8 Protein Arginine Methyltransferase in Neurons.Life (Basel, Switzerland) · 2021Review
- Non-Histone Arginine Methylation by Protein Arginine Methyltransferases.Current protein & peptide science · 2020Review
- Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.Cellular and molecular life sciences : CMLS · 2019Review
- Article
- Mechanisms and Inhibitors of Histone Arginine Methylation.Chemical record (New York, N.Y.) · 2018Review
- The Major Protein Arginine Methyltransferase inThe Journal of biological chemistry · 2017Article
- Transient Kinetics Define a Complete Kinetic Model for Protein Arginine Methyltransferase 1.The Journal of biological chemistry · 2016Article
- Small Molecule Inhibitors of Protein Arginine Methyltransferases.Expert opinion on investigational drugs · 2016Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric dimethylation of various proteins, and their dysregulations often correlate with tumorigenesis or developmental deficiency. Recent studies have focused on the in vivo substrate identification and the enzyme mechanism with peptide substrates. However, how PRMTs recognize substrates at the protein level remains unknown. PRMT8 is one of the least characterized type I PRMTs, and its crystal structure has not been reported. Here, we report the crystal structure of the PRMT8:SAH complex, identify a new non-histone protein substrate NIFK, and uncover a previously unknown regulatory region specifically required for recognizing NIFK. Instead of the canonical dimeric structure for other type I PRMTs, PRMT8 exists as a tetramer in solution. Using X-ray crystallography in combination with small-angle X-ray scattering experiments, the dimer of dimers architecture in which two PRMT8 dimers are held together mainly by β strand interactions was proposed. Mutation of PRMT8-β15 impedes the methylation of NIFK but still allows methylation of the histone H2A/H2B dimer or a peptide substrate, suggesting a possible structural basis for recognition of protein substrates. Lastly, we observed two PRMT8 dimer orientations resulting in open (without SAH) and closed (with SAH bound) conformations. The comparison between open and closed conformations may provide useful information for PRMT1/8 inhibitor design.
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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.