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Journal articles on the topic 'H3K4 methyltransferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 18 February 2022

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1

Umezawa, Ryohei, Masanobu Yamada, Kazuhiko Horiguchi, et al. "Aberrant Histone Modifications at the Thyrotropin-Releasing Hormone Gene in Resistance to Thyroid Hormone: Analysis of F455S Mutant Thyroid Hormone Receptor." Endocrinology 150, no. 7 (2009): 3425–32. http://dx.doi.org/10.1210/en.2008-1738.

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We reported a novel mutation of thyroid hormone receptor (TR)-β, F455S, in a patient with pituitary resistance to thyroid hormone (RTH), who showed impaired release of nuclear receptor corepressor and abnormal histone deacetylation. In the present study, we further analyzed the histone modifications and the dynamics of TR and RNA polymerase II on the TRH gene. The lysine residues 9 (H3K9) and 14 (K14) of the histone H3 were acetylated in the absence of thyroid hormone (TH), and addition of TH caused a temporary deacetylation of both residues. Although H3K4 was di- and trimethylated in the abse

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2

Gregory, Gregory D., Christopher R. Vakoc, Tanya Rozovskaia, et al. "Mammalian ASH1L Is a Histone Methyltransferase That Occupies the Transcribed Region of Active Genes." Molecular and Cellular Biology 27, no. 24 (2007): 8466–79. http://dx.doi.org/10.1128/mcb.00993-07.

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ABSTRACT Histone lysine methylation regulates genomic functions, including gene transcription. Previous reports found various degrees of methylation at H3K4, H3K9, and H4K20 within the transcribed region of active mammalian genes. To identify the enzymes responsible for placing these modifications, we examined ASH1L, the mammalian homolog of the Drosophila melanogaster Trithorax group (TrxG) protein Ash1. Drosophila Ash1 has been reported to methylate H3K4, H3K9, and H4K20 at its target sites. Here we demonstrate that mammalian ASH1L associates with the transcribed region of all active genes e

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Yang, Liu, Mingli Jin, and Kwang Won Jeong. "Histone H3K4 Methyltransferases as Targets for Drug-Resistant Cancers." Biology 10, no. 7 (2021): 581. http://dx.doi.org/10.3390/biology10070581.

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The KMT2 (MLL) family of proteins, including the major histone H3K4 methyltransferase found in mammals, exists as large complexes with common subunit proteins and exhibits enzymatic activity. SMYD, another H3K4 methyltransferase, and SET7/9 proteins catalyze the methylation of several non-histone targets, in addition to histone H3K4 residues. Despite these structural and functional commonalities, H3K4 methyltransferase proteins have specificity for their target genes and play a role in the development of various cancers as well as in drug resistance. In this review, we examine the overall role

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Napieralski, Rudolf, Ernst Wagner, Harry Gebhard, et al. "Alternation of histone and DNA methylation in human atherosclerotic carotid plaques." Thrombosis and Haemostasis 114, no. 08 (2015): 390–402. http://dx.doi.org/10.1160/th14-10-0852.

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SummaryLittle is known about epigenetics and its possible role in atherosclerosis. We here analysed histone and DNA methylation and the expression of corresponding methyltransferases in early and advanced human atherosclerotic carotid lesions in comparison to healthy carotid arteries. Western Blotting was performed on carotid plaques from our biobank with early (n=60) or advanced (n=60) stages of atherosclerosis and healthy carotid arteries (n=12) to analyse di-methylation patterns of histone H3 at positions K4, K9 and K27. In atherosclerotic lesions, di-methylation of H3K4 was unaltered and t

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Kwon, Minjung, Kihyun Park, Kwangbeom Hyun, et al. "H2B ubiquitylation enhances H3K4 methylation activities of human KMT2 family complexes." Nucleic Acids Research 48, no. 10 (2020): 5442–56. http://dx.doi.org/10.1093/nar/gkaa317.

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Abstract In mammalian cells, distinct H3K4 methylation states are created by deposition of methyl groups by multiple complexes of histone lysine methyltransferase 2 (KMT2) family proteins. For comprehensive analyses that directly compare the catalytic properties of all six human KMT2 complexes, we employed a biochemically defined system reconstituted with recombinant KMT2 core complexes (KMT2CoreCs) containing minimal components required for nucleosomal H3K4 methylation activity. We found that each KMT2CoreC generates distinct states and different levels of H3K4 methylation, and except for MLL

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Wang, Pengbo, Marcel Dreger, Elena Madrazo, et al. "WDR5 modulates cell motility and morphology and controls nuclear changes induced by a 3D environment." Proceedings of the National Academy of Sciences 115, no. 34 (2018): 8581–86. http://dx.doi.org/10.1073/pnas.1719405115.

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Cell migration through extracellular matrices requires nuclear deformation, which depends on nuclear stiffness. In turn, chromatin structure contributes to nuclear stiffness, but the mechanosensing pathways regulating chromatin during cell migration remain unclear. Here, we demonstrate that WD repeat domain 5 (WDR5), an essential component of H3K4 methyltransferase complexes, regulates cell polarity, nuclear deformability, and migration of lymphocytes in vitro and in vivo, independent of transcriptional activity, suggesting nongenomic functions for WDR5. Similarly, depletion of RbBP5 (another

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7

Zhang, Zhiren, Yanhui Zhai, Xiaoling Ma, et al. "Down-Regulation of H3K4me3 by MM-102 Facilitates Epigenetic Reprogramming of Porcine Somatic Cell Nuclear Transfer Embryos." Cellular Physiology and Biochemistry 45, no. 4 (2018): 1529–40. http://dx.doi.org/10.1159/000487579.

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Background/Aims: Aberrantly high levels of H3K4me3, caused by incomplete epigenetic reprogramming, likely cause a low efficiency of somatic cell nuclear transfer (SCNT). Smal molecule inhibitors aimed at epigenetic modification can be used to improve porcine SCNT embryo development. In this study, we examined the effects of MM-102, an H3K4 histone methyltransferase inhibitor, on porcine SCNT preimplantation embryos to investigate the mechanism by which H3K4 methylation regulated global epigenetic reprograming during SCNT. Methods: MM-102 was added to the SCNT embryos culture system and the glo

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8

Li, Xingguo, Shaohua Wang, Ying Li, Yi Qiu, and Suming Huang. "Chromatin Boundaries Require the Functional Cooperation Between hSET1 and NURF Complexes." Blood 116, no. 21 (2010): 646. http://dx.doi.org/10.1182/blood.v116.21.646.646.

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Abstract Abstract 646 Chromatin modification and remodeling activities play a central role in organizing nuclear functions in eukaryotic genome. Chromatin domains with characteristic epigenetic marks are organized by chromatin insulator. The chicken b-globin insulator, 5′HS4, is an excellent model system to study how insulator maintains gene function and prevents the encroachment of repressive heterochromatin. We showed previously that USF1/2 bound 5′HS4 insulator mediates chromatin barrier activity by recruiting and organizing active histone modifications in the chicken b-globin locus. Howeve

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Klonou, Alexia, Sarantis Chlamydas, and Christina Piperi. "Structure, Activity and Function of the MLL2 (KMT2B) Protein Lysine Methyltransferase." Life 11, no. 8 (2021): 823. http://dx.doi.org/10.3390/life11080823.

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The Mixed Lineage Leukemia 2 (MLL2) protein, also known as KMT2B, belongs to the family of mammalian histone H3 lysine 4 (H3K4) methyltransferases. It is a large protein of 2715 amino acids, widely expressed in adult human tissues and a paralog of the MLL1 protein. MLL2 contains a characteristic C-terminal SET domain responsible for methyltransferase activity and forms a protein complex with WRAD (WDR5, RbBP5, ASH2L and DPY30), host cell factors 1/2 (HCF 1/2) and Menin. The MLL2 complex is responsible for H3K4 trimethylation (H3K4me3) on specific gene promoters and nearby cis-regulatory sites,

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10

Cao, Fang, Elizabeth C. Townsend, Hacer Karatas, et al. "Targeting MLL1 H3K4 Methyltransferase Activity in Mixed-Lineage Leukemia." Molecular Cell 53, no. 2 (2014): 247–61. http://dx.doi.org/10.1016/j.molcel.2013.12.001.

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11

Jang, Younghoon, Chaochen Wang, Lenan Zhuang, Chengyu Liu, and Kai Ge. "H3K4 Methyltransferase Activity Is Required for MLL4 Protein Stability." Journal of Molecular Biology 429, no. 13 (2017): 2046–54. http://dx.doi.org/10.1016/j.jmb.2016.12.016.

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12

Hsu, Peter L., Heng Li, Ho-Tak Lau, et al. "Crystal Structure of the COMPASS H3K4 Methyltransferase Catalytic Module." Cell 174, no. 5 (2018): 1106–16. http://dx.doi.org/10.1016/j.cell.2018.06.038.

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13

Liu, Chunchun, Yuxue Zhang, Yongfan Hou, et al. "PAQR3 modulates H3K4 trimethylation by spatial modulation of the regulatory subunits of COMPASS-like complexes in mammalian cells." Biochemical Journal 467, no. 3 (2015): 415–24. http://dx.doi.org/10.1042/bj20141392.

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Histone modification plays important roles in many biological processes such as development and carcinogenesis. Methylation of histone H3 lysine 4 (H3K4) is commonly associated with transcriptional activation of genes. H3K4 methylation in mammalian cells is carried out by COMPASS (complex of proteins associated with Set1)-like complexes that are composed of catalytic subunits such as MLL1 (mixed-lineage leukaemia 1) and multiple regulatory subunits in which WDR5 (WD40 repeat-containing protein 5), RBBP5 (retinoblastoma-binding protein 5), ASH2 (absent, small or homoeotic discs 2) and DPY30 [co

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14

Nightingale, Karl P., Susanne Gendreizig, Darren A. White, Charlotte Bradbury, Florian Hollfelder, and Bryan M. Turner. "Cross-talk between Histone Modifications in Response to Histone Deacetylase Inhibitors." Journal of Biological Chemistry 282, no. 7 (2006): 4408–16. http://dx.doi.org/10.1074/jbc.m606773200.

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Histones are subject to a wide variety of post-translational modifications that play a central role in gene activation and silencing. We have used histone modification-specific antibodies to demonstrate that two histone modifications involved in gene activation, histone H3 acetylation and H3 lysine 4 methylation, are functionally linked. This interaction, in which the extent of histone H3 acetylation determines both the abundance and the “degree” of H3K4 methylation, plays a major role in the epigenetic response to histone deacetylase inhibitors. A combination of in vivo knockdown experiments

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15

Li, Xingguo, Xin Hu, Gary Felsenfeld та Suming Huang. "USF1 Recruits hSET1 Complex and Is Important for Maintaining Active Chromatin Domains in the β-Globin Locus." Blood 110, № 11 (2007): 274. http://dx.doi.org/10.1182/blood.v110.11.274.274.

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Abstract The chicken β-globin insulator element acts as a barrier to the encroachment of chromosomal silencing. This barrier insulator prevents the spread of a 16 Kb domain of condensed chromatin which lies immediately upstream of the β-globin genes in the chicken genome. We have previously shown that the transcription factors USF1/2 mediate the barrier activity by binding to the 5′HS4 insulator element of the chicken β-globin locus and maintaining a local active chromatin structure. In the mouse β-globin locus, USFs also play a critical role in regulating the developmental stage-specific tran

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16

Kaczmarek Michaels, Katarzyna, Salwa Mohd Mostafa, Julia Ruiz Capella, and Claire L. Moore. "Regulation of alternative polyadenylation in the yeast Saccharomyces cerevisiae by histone H3K4 and H3K36 methyltransferases." Nucleic Acids Research 48, no. 10 (2020): 5407–25. http://dx.doi.org/10.1093/nar/gkaa292.

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Abstract Adjusting DNA structure via epigenetic modifications, and altering polyadenylation (pA) sites at which precursor mRNA is cleaved and polyadenylated, allows cells to quickly respond to environmental stress. Since polyadenylation occurs co-transcriptionally, and specific patterns of nucleosome positioning and chromatin modifications correlate with pA site usage, epigenetic factors potentially affect alternative polyadenylation (APA). We report that the histone H3K4 methyltransferase Set1, and the histone H3K36 methyltransferase Set2, control choice of pA site in Saccharomyces cerevisiae

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17

Shah, Kushani, Gwendalyn D. King, and Hao Jiang. "A chromatin modulator sustains self-renewal and enables differentiation of postnatal neural stem and progenitor cells." Journal of Molecular Cell Biology 12, no. 1 (2019): 4–16. http://dx.doi.org/10.1093/jmcb/mjz036.

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Abstract It remains unknown whether H3K4 methylation, an epigenetic modification associated with gene activation, regulates fate determination of the postnatal neural stem and progenitor cells (NSPCs). By inactivating the Dpy30 subunit of the major H3K4 methyltransferase complexes in specific regions of mouse brain, we demonstrate a crucial role of efficient H3K4 methylation in maintaining both the self-renewal and differentiation capacity of postnatal NSPCs. Dpy30 deficiency disrupts development of hippocampus and especially the dentate gyrus and subventricular zone, the major regions for pos

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18

Hallson, Graham, Robert E. Hollebakken, Taosui Li, et al. "dSet1 Is the Main H3K4 Di- and Tri-Methyltransferase ThroughoutDrosophilaDevelopment." Genetics 190, no. 1 (2011): 91–100. http://dx.doi.org/10.1534/genetics.111.135863.

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19

Wang, Chaochen, Ji-Eun Lee, Binbin Lai, et al. "Enhancer priming by H3K4 methyltransferase MLL4 controls cell fate transition." Proceedings of the National Academy of Sciences 113, no. 42 (2016): 11871–76. http://dx.doi.org/10.1073/pnas.1606857113.

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Transcriptional enhancers control cell-type–specific gene expression. Primed enhancers are marked by histone H3 lysine 4 (H3K4) mono/di-methylation (H3K4me1/2). Active enhancers are further marked by H3K27 acetylation (H3K27ac). Mixed-lineage leukemia 4 (MLL4/KMT2D) is a major enhancer H3K4me1/2 methyltransferase with functional redundancy with MLL3 (KMT2C). However, its role in cell fate maintenance and transition is poorly understood. Here, we show in mouse embryonic stem cells (ESCs) that MLL4 associates with, but is surprisingly dispensable for the maintenance of, active enhancers of cell-

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Tamura, Ryo, Shigehiro Doi, Ayumu Nakashima, et al. "Inhibition of the H3K4 methyltransferase SET7/9 ameliorates peritoneal fibrosis." PLOS ONE 13, no. 5 (2018): e0196844. http://dx.doi.org/10.1371/journal.pone.0196844.

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21

Dou, Yali, Thomas A. Milne, Alexander J. Ruthenburg, et al. "Regulation of MLL1 H3K4 methyltransferase activity by its core components." Nature Structural & Molecular Biology 13, no. 8 (2006): 713–19. http://dx.doi.org/10.1038/nsmb1128.

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22

Wu, Hong, Weihong Zheng, Mohammad S. Eram, et al. "Structural basis of arginine asymmetrical dimethylation by PRMT6." Biochemical Journal 473, no. 19 (2016): 3049–63. http://dx.doi.org/10.1042/bcj20160537.

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PRMT6 is a type I protein arginine methyltransferase, generating the asymmetric dimethylarginine mark on proteins such as histone H3R2. Asymmetric dimethylation of histone H3R2 by PRMT6 acts as a repressive mark that antagonizes trimethylation of H3 lysine 4 by the MLL histone H3K4 methyltransferase. PRMT6 is overexpressed in several cancer types, including prostate, bladder and lung cancers; therefore, it is of great interest to develop potent and selective inhibitors for PRMT6. Here, we report the synthesis of a potent bisubstrate inhibitor GMS [6′-methyleneamine sinefungin, an analog of sin

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23

Xiao, Tiaojiang, Yoichiro Shibata, Bhargavi Rao, et al. "The RNA Polymerase II Kinase Ctk1 Regulates Positioning of a 5′ Histone Methylation Boundary along Genes." Molecular and Cellular Biology 27, no. 2 (2006): 721–31. http://dx.doi.org/10.1128/mcb.01628-06.

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ABSTRACT In yeast and other eukaryotes, the histone methyltransferase Set1 mediates methylation of lysine 4 on histone H3 (H3K4me). This modification marks the 5′ end of transcribed genes in a 5′-to-3′ tri- to di- to monomethyl gradient and promotes association of chromatin-remodeling and histone-modifying enzymes. Here we show that Ctk1, the serine 2 C-terminal domain (CTD) kinase for RNA polymerase II (RNAP II), regulates H3K4 methylation. We found that CTK1 deletion nearly abolished H3K4 monomethylation yet caused a significant increase in H3K4 di- and trimethylation. Both in individual gen

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Karakkat, Jimsheena V., Suneesh Kaimala, Sreejisha P. Sreedharan, et al. "The metabolic sensor PASK is a histone 3 kinase that also regulates H3K4 methylation by associating with H3K4 MLL2 methyltransferase complex." Nucleic Acids Research 47, no. 19 (2019): 10086–103. http://dx.doi.org/10.1093/nar/gkz786.

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Abstract The metabolic sensor Per-Arnt-Sim (Pas) domain-containing serine/threonine kinase (PASK) is expressed predominantly in the cytoplasm of different cell types, although a small percentage is also expressed in the nucleus. Herein, we show that the nuclear PASK associates with the mammalian H3K4 MLL2 methyltransferase complex and enhances H3K4 di- and tri-methylation. We also show that PASK is a histone kinase that phosphorylates H3 at T3, T6, S10 and T11. Taken together, these results suggest that PASK regulates two different H3 tail modifications involving H3K4 methylation and H3 phosph

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Kim, Dae-Hwan, Jeongkyung Lee, Bora Lee, and Jae W. Lee. "ASCOM Controls Farnesoid X Receptor Transactivation through Its Associated Histone H3 Lysine 4 Methyltransferase Activity." Molecular Endocrinology 23, no. 10 (2009): 1556–62. http://dx.doi.org/10.1210/me.2009-0099.

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Abstract Activating signal cointegrator-2 (ASC-2), a coactivator of multiple nuclear receptors and transcription factors, belongs to a steady-state complex named ASCOM (for ASC-2 complex), which contains histone H3 lysine 4 (H3K4) methyltransferase MLL3 or its paralog MLL4. ASC-2 binds to many nuclear receptors in a ligand-dependent manner through its two LxxLL motifs. Here we show that the first LxxLL motif of ASC-2 shows relatively weak but specific interaction with the nuclear receptor farnesoid X receptor (FXR) and that ASCOM plays crucial roles in FXR transactivation. Our results reveal t

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Dreijerink, Koen M. A., Radhika A. Varier, Olivier van Beekum та ін. "The Multiple Endocrine Neoplasia Type 1 (MEN1) Tumor Suppressor Regulates Peroxisome Proliferator-Activated Receptor γ-Dependent Adipocyte Differentiation". Molecular and Cellular Biology 29, № 18 (2009): 5060–69. http://dx.doi.org/10.1128/mcb.01001-08.

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ABSTRACT Menin, the product of the MEN1 (multiple endocrine neoplasia type 1) tumor suppressor gene, is involved in activation of gene transcription as part of an MLL1 (mixed-lineage leukemia 1)/MLL2 (KMT2A/B)-containing protein complex which harbors methyltransferase activity for lysine 4 of histone H3 (H3K4). As MEN1 patients frequently develop lipomas and peroxisome proliferator-activated receptor γ (PPARγ) is expressed in several MEN1-related tumor types, we investigated regulation of PPARγ activity by menin. We found that menin is required for adipocyte differentiation of murine 3T3-L1 ce

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Butler, Jill S., Cecilia I. Zurita-Lopez, Steven G. Clarke, Mark T. Bedford, and Sharon Y. R. Dent. "Protein-arginine Methyltransferase 1 (PRMT1) Methylates Ash2L, a Shared Component of Mammalian Histone H3K4 Methyltransferase Complexes." Journal of Biological Chemistry 286, no. 14 (2011): 12234–44. http://dx.doi.org/10.1074/jbc.m110.202416.

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Papaefthimiou, D., and A. S. Tsaftaris. "Characterization of a drought inducible trithorax-like H3K4 methyltransferase from barley." Biologia plantarum 56, no. 4 (2012): 683–92. http://dx.doi.org/10.1007/s10535-012-0125-z.

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Qu, Qianhui, Yoh-hei Takahashi, Yidai Yang, et al. "Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex." Cell 174, no. 5 (2018): 1117–26. http://dx.doi.org/10.1016/j.cell.2018.07.020.

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Daniel, Jeremy A., and André Nussenzweig. "Roles for histone H3K4 methyltransferase activities during immunoglobulin class-switch recombination." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1819, no. 7 (2012): 733–38. http://dx.doi.org/10.1016/j.bbagrm.2012.01.019.

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Nan, Zi, Weiwei Yang, Jialan Lyu, et al. "Drosophila Hcf regulates the Hippo signaling pathway via association with the histone H3K4 methyltransferase Trr." Biochemical Journal 476, no. 4 (2019): 759–68. http://dx.doi.org/10.1042/bcj20180717.

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Abstract Control of organ size is a fundamental aspect in biology and plays important roles in development. The Hippo pathway is a conserved signaling cascade that controls tissue and organ size through the regulation of cell proliferation and apoptosis. Here, we report on the roles of Hcf (host cell factor), the Drosophila homolog of Host cell factor 1, in regulating the Hippo signaling pathway. Loss-of-Hcf function causes tissue undergrowth and the down-regulation of Hippo target gene expression. Genetic analysis reveals that Hcf is required for Hippo pathway-mediated overgrowth. Mechanistic

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Wu, Hong, Nikolas Mathioudakis, Boubou Diagouraga, et al. "Molecular Basis for the Regulation of the H3K4 Methyltransferase Activity of PRDM9." Cell Reports 5, no. 1 (2013): 13–20. http://dx.doi.org/10.1016/j.celrep.2013.08.035.

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Jozwik, Kamila M., Igor Chernukhin, Aurelien A. Serandour, Sankari Nagarajan, and Jason S. Carroll. "FOXA1 Directs H3K4 Monomethylation at Enhancers via Recruitment of the Methyltransferase MLL3." Cell Reports 17, no. 10 (2016): 2715–23. http://dx.doi.org/10.1016/j.celrep.2016.11.028.

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Issaeva, Irina, Yulia Zonis, Tanya Rozovskaia, et al. "Knockdown of ALR (MLL2) Reveals ALR Target Genes and Leads to Alterations in Cell Adhesion and Growth." Molecular and Cellular Biology 27, no. 5 (2006): 1889–903. http://dx.doi.org/10.1128/mcb.01506-06.

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ABSTRACT ALR (MLL2) is a member of the human MLL family, which belongs to a larger SET1 family of histone methyltransferases. We found that ALR is present within a stable multiprotein complex containing a cohort of proteins shared with other SET1 family complexes and several unique components, such as PTIP and the jumonji family member UTX. Like other complexes formed by SET1 family members, the ALR complex exhibited strong H3K4 methyltransferase activity, conferred by the ALR SET domain. By generating ALR knockdown cell lines and comparing their expression profiles to that of control cells, w

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Deng, Changwang, Ying Li, Shermi Liang, et al. "Role of hSET1 Complex in Epigenetic Controls of HoxB4 Expression and Development of Hematopoietic Stem Cells." Blood 118, no. 21 (2011): 212. http://dx.doi.org/10.1182/blood.v118.21.212.212.

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Abstract Abstract 212 Hox genes play an important role in embryonic development and are sequentially activated in a temporal and spatial fashion. Among them, HoxB4 regulates the self-renewal ability of adult and embryonic hematopoietic stem cells. It was shown that USF proteins positively regulate the transcription of HoxB4 gene. However, the epigenetic mechanism specifically controlling HoxB4 transcription during HSC formation remains unknown. In this report, we found that USF1 interacts with histone H3K4 methylatransferase SET1 complex, but not MLL proteins. The interaction is mediated by SE

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Francis, M., G. Gopinathan, A. Salapatas та ін. "SETD1 and NF-κB Regulate Periodontal Inflammation through H3K4 Trimethylation". Journal of Dental Research 99, № 13 (2020): 1486–93. http://dx.doi.org/10.1177/0022034520939029.

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The inflammatory response to periodontal pathogens is dynamically controlled by the chromatin state on inflammatory gene promoters. In the present study, we have focused on the effect of the methyltransferase SETD1B on histone H3 lysine K4 (H3K4) histone trimethylation on inflammatory gene promoters. Experiments were based on 3 model systems: 1) an in vitro periodontal ligament (PDL) cell culture model for the study of SETD1 function as it relates to histone methylation and inflammatory gene expression using Porphyromonas gingivalis lipopolysaccharide (LPS) as a pathogen, 2) a subcutaneous imp

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Tate, Courtney M., Jeong-Heon Lee, and David G. Skalnik. "CXXC finger protein 1 restricts the Setd1A histone H3K4 methyltransferase complex to euchromatin." FEBS Journal 277, no. 1 (2009): 210–23. http://dx.doi.org/10.1111/j.1742-4658.2009.07475.x.

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Rahnamoun, Homa, Juyeong Hong, Zhengxi Sun, Jihoon Lee, Hanbin Lu, and Shannon M. Lauberth. "Mutant p53 regulates enhancer-associated H3K4 monomethylation through interactions with the methyltransferase MLL4." Journal of Biological Chemistry 293, no. 34 (2018): 13234–46. http://dx.doi.org/10.1074/jbc.ra118.003387.

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Yang, Di, Zhenghua Su, Gang Wei, et al. "H3K4 Methyltransferase Smyd3 Mediates Vascular Smooth Muscle Cell Proliferation, Migration, and Neointima Formation." Arteriosclerosis, Thrombosis, and Vascular Biology 41, no. 6 (2021): 1901–14. http://dx.doi.org/10.1161/atvbaha.121.314689.

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Objective: Smyd3 (SET and MYND domain-containing protein 3) is an H3K4 (histone H3 lysine 4) dimethyltransferase and trimethyltransferase that activates the transcription of oncogenes and cell cycle genes in human cancer cells. We discovered its overexpression in proliferative vascular smooth muscle cells (VSMCs). However, whether Smyd3 plays a role in vascular remodeling remains unanswered. The objective of this study is to investigate the role and underlying mechanism of Smyd3 in phenotypic transition of VSMCs (such as proliferation and migration) and vascular remodeling (such as neointima f

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Leung, Amy, Ivelisse Cajigas, Peilin Jia, et al. "Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat." Molecular Biology of the Cell 22, no. 15 (2011): 2741–53. http://dx.doi.org/10.1091/mbc.e11-05-0426.

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In Saccharomyces cerevisiae, ubiquitylation of histone H2B signals methylation of histone H3 at lysine residues 4 (K4) and 79. These modifications occur at active genes but are believed to stabilize silent chromatin by limiting movement of silencing proteins away from heterochromatin domains. In the course of studying atypical phenotypes associated with loss of H2B ubiquitylation/H3K4 methylation, we discovered that these modifications are also required for cell wall integrity at high temperatures. We identified the silencing protein Sir4 as a dosage suppressor of loss of H2B ubiquitylation, a

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Zraly, Claudia B., Abdul Zakkar, John Hertenstein Perez, et al. "The Drosophila MLR COMPASS complex is essential for programming cis-regulatory information and maintaining epigenetic memory during development." Nucleic Acids Research 48, no. 7 (2020): 3476–95. http://dx.doi.org/10.1093/nar/gkaa082.

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Abstract The MLR COMPASS complex monomethylates H3K4 that serves to epigenetically mark transcriptional enhancers to drive proper gene expression during animal development. Chromatin enrichment analyses of the Drosophila MLR complex reveals dynamic association with promoters and enhancers in embryos with late stage enrichments biased toward both active and poised enhancers. RNAi depletion of the Cmi (also known as Lpt) subunit that contains the chromatin binding PHD finger domains attenuates enhancer functions, but unexpectedly results in inappropriate enhancer activation during stages when ho

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Chaturvedi, C. P., B. Somasundaram, K. Singh, et al. "Maintenance of gene silencing by the coordinate action of the H3K9 methyltransferase G9a/KMT1C and the H3K4 demethylase Jarid1a/KDM5A." Proceedings of the National Academy of Sciences 109, no. 46 (2012): 18845–50. http://dx.doi.org/10.1073/pnas.1213951109.

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Zhao, Shuai, Kelly N. Chuh, Baichao Zhang, et al. "Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout." Proceedings of the National Academy of Sciences 118, no. 6 (2021): e2016742118. http://dx.doi.org/10.1073/pnas.2016742118.

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Serotonylation of glutamine 5 on histone H3 (H3Q5ser) was recently identified as a permissive posttranslational modification that coexists with adjacent lysine 4 trimethylation (H3K4me3). While the resulting dual modification, H3K4me3Q5ser, is enriched at regions of active gene expression in serotonergic neurons, the molecular outcome underlying H3K4me3–H3Q5ser crosstalk remains largely unexplored. Herein, we examine the impact of H3Q5ser on the readers, writers, and erasers of H3K4me3. All tested H3K4me3 readers retain binding to the H3K4me3Q5ser dual modification. Of note, the PHD finger of

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Butler, Jill Sergesketter, Jeong-Heon Lee, and David G. Skalnik. "CFP1 Interacts with DNMT1 Independently of Association with the Setd1 Histone H3K4 Methyltransferase Complexes." DNA and Cell Biology 27, no. 10 (2008): 533–43. http://dx.doi.org/10.1089/dna.2007.0714.

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Kim, D. H., Z. Tang, M. Shimada, et al. "Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes." Molecular and Cellular Biology 33, no. 24 (2013): 4936–46. http://dx.doi.org/10.1128/mcb.00601-13.

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Wang, Xiang, Lingao Ju, Jiadong Fan, et al. "Histone H3K4 methyltransferase Mll1 regulates protein glycosylation and tunicamycin-induced apoptosis through transcriptional regulation." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1843, no. 11 (2014): 2592–602. http://dx.doi.org/10.1016/j.bbamcr.2014.06.013.

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Robert, Valérie J., Marine G. Mercier, Cécile Bedet, et al. "The SET-2/SET1 Histone H3K4 Methyltransferase Maintains Pluripotency in the Caenorhabditis elegans Germline." Cell Reports 9, no. 2 (2014): 443–50. http://dx.doi.org/10.1016/j.celrep.2014.09.018.

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Han, Jianming, Tingting Li, Yanjing Li, et al. "The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex." Nucleic Acids Research 47, no. 19 (2019): 10426–38. http://dx.doi.org/10.1093/nar/gkz819.

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Abstract The Mixed Lineage Leukemia protein 1 (MLL1) plays an essential role in the maintenance of the histone H3 lysine 4 (H3K4) methylation status for gene expression during differentiation and development. The methyltransferase activity of MLL1 is regulated by three conserved core subunits, WDR5, RBBP5 and ASH2L. Here, we determined the structure of human RBBP5 and demonstrated its role in the assembly and regulation of the MLL1 complex. We identified an internal interaction between the WD40 propeller and the C-terminal distal region in RBBP5, which assisted the maintenance of the compact c

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Wu, Jugang, Jiwei Yu, and Yan Gu. "SETD1A to induce epithelial-mesenchymal transition to promote invasion and metastasis through epigenetic reprogramming of snail in gastric cancer." Journal of Clinical Oncology 39, no. 3_suppl (2021): 241. http://dx.doi.org/10.1200/jco.2021.39.3_suppl.241.

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241 Background: Aberrant epigenetic modification induces oncogenes expression and promotes cancer development. The histone lysine methyltransferase SETD1A, which specifically methylates H3K4, is involved in tumor growth and metastasis, and its ectopic expression has been detected in aggressive malignancies. Our previous study had reported that SETD1A promoted gastric cancer (GC) proliferation and tumorigenesis. However, the function and molecular mechanisms of SETD1A in GC metastasis remain to be elucidated. Methods: Transwell migration and invasion assay were performed to determine GC cell mi

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Jin, Yi, Amy M. Rodriguez, Julie D. Stanton, Ana A. Kitazono, and John J. Wyrick. "Simultaneous Mutation of Methylated Lysine Residues in Histone H3 Causes Enhanced Gene Silencing, Cell Cycle Defects, and Cell Lethality in Saccharomyces cerevisiae." Molecular and Cellular Biology 27, no. 19 (2007): 6832–41. http://dx.doi.org/10.1128/mcb.00745-07.

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ABSTRACT The methylation of specific lysine residues in histone H3 is integral to transcription regulation; however, little is known about how combinations of methylated lysine residues act in concert to regulate genome-wide transcription. We have systematically mutated methylated histone lysine residues in yeast and found that the triple mutation of H3K4, H3K36, and H3K79 to arginine (H3 K4,36,79R) is lethal. The histone H3 K4,36,79R mutant causes a mitotic cell cycle delay and a progressive transcription defect that initiates in telomere regions and then spreads into the chromosome. This eff

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