ArticleThe Journal of biological chemistry2011
A novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complex.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 52 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
52 citing papers in PubMed, 79 citations in OpenAlex.
- Probing the Cancer Mutational Landscape of KMT2 Regulatory Subunits.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Insights into WDR5: unveiling its functions, regulation, and impact on skeletal muscle.Epigenetics · 2025Review
- lncCPSET1 acts as a scaffold for MLL2/COMPASS to regulate Bmp4 and promote the formation of chicken primordial germ cells.Molecular genetics and genomics : MGG · 2024Article
- An acetylation-mediated chromatin switch governs H3K4 methylation read-write capability.eLife · 2023Article
- Hierarchical assembly of the MLL1 core complex regulates H3K4 methylation and is dependent on temperature and component concentration.The Journal of biological chemistry · 2023Article
- Parallel functional annotation of cancer-associated missense mutations in histone methyltransferases.Scientific reports · 2022Article
- Multistate structures of the MLL1-WRAD complex bound to H2B-ubiquitinated nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- PHF20 is crucial for epigenetic control of starvation-induced autophagy through enhancer activation.Nucleic acids research · 2022Article
- Article
- The role of Trithorax family regulating osteogenic and Chondrogenic differentiation in mesenchymal stem cells.Cell proliferation · 2022Review
- MLL1 is regulated by KSHV LANA and is important for virus latency.Nucleic acids research · 2021Article
- H3K4 Methylation in Aging and Metabolism.Epigenomes · 2021Review
- Kinetics of the multitasking high-affinity Win binding site of WDR5 in restricted and unrestricted conditions.The Biochemical journal · 2021Article
- H3K4me2 regulates the recovery of protein biosynthesis and homeostasis following DNA damage.Nature structural & molecular biology · 2020Article
- Insights on the regulation of the MLL/SET1 family histone methyltransferases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020Review
- Physical and functional interaction between SET1/COMPASS complex component CFP-1 and a Sin3S HDAC complex in C. elegans.Nucleic acids research · 2019Article
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
- Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin.Cells · 2018Review
- H3K4 Methyltransferase Activity Is Required for MLL4 Protein Stability.Journal of molecular biology · 2017Article
- Targeting human SET1/MLL family of proteins.Protein science : a publication of the Protein Society · 2017Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Gene expression within the context of eukaryotic chromatin is regulated by enzymes that catalyze histone lysine methylation. Histone lysine methyltransferases that have been identified to date possess the evolutionarily conserved SET or Dot1-like domains. We previously reported the identification of a new multi-subunit histone H3 lysine 4 methyltransferase lacking homology to the SET or Dot1 family of histone lysine methyltransferases. This enzymatic activity requires a complex that includes WRAD (WDR5, RbBP5, Ash2L, and DPY-30), a complex that is part of the MLL1 (mixed lineage leukemia protein-1) core complex but that also exists independently of MLL1 in the cell. Here, we report that the minimal complex required for WRAD enzymatic activity includes WDR5, RbBP5, and Ash2L and that DPY-30, although not required for enzymatic activity, increases the histone substrate specificity of the WRAD complex. We also show that WRAD requires zinc for catalytic activity, displays Michaelis-Menten kinetics, and is inhibited by S-adenosyl-homocysteine. In addition, we demonstrate that WRAD preferentially methylates lysine 4 of histone H3 within the context of the H3/H4 tetramer but does not methylate nucleosomal histone H3 on its own. In contrast, we find that MLL1 and WRAD are required for nucleosomal histone H3 methylation, and we provide evidence suggesting that each plays distinct structural and catalytic roles in the recognition and methylation of a nucleosome substrate. Our results indicate that WRAD is a new H3K4 methyltransferase with functions that include regulating the substrate and product specificities of the MLL1 core complex.
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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.