Relevant bibliographies by topics / Protein arginine methyltransferase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Protein arginine methyltransferase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Protein arginine methyltransferase"

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Yan, Dongsheng, Yong Zhang, Lifang Niu, Yi Yuan, and Xiaofeng Cao. "Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana." Biochemical Journal 408, no. 1 (October 29, 2007): 113–21. http://dx.doi.org/10.1042/bj20070786.

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Arginine methylation of histone H3 and H4 plays important roles in transcriptional regulation in eukaryotes such as yeasts, fruitflies, nematode worms, fish and mammals; however, less is known in plants. In the present paper, we report the identification and characterization of two Arabidopsis thaliana protein arginine N-methyltransferases, AtPRMT1a and AtPRMT1b, which exhibit high homology with human PRMT1. Both AtPRMT1a and AtPRMT1b methylated histone H4, H2A, and myelin basic protein in vitro. Site-directed mutagenesis of the third arginine (R3) on the N-terminus of histone H4 to lysine (H4R3N) completely abolished the methylation of histone H4. When fused to GFP (green fluorescent protein), both methyltransferases localized to the cytoplasm as well as to the nucleus. Consistent with their subcellular distribution, GST (glutathione transferase) pull-down assays revealed an interaction between the two methyltransferases, suggesting that both proteins may act together in a functional unit. In addition, we demonstrated that AtFib2 (Arabidopsis thaliana fibrillarin 2), an RNA methyltransferase, is a potential substrate for AtPRMT1a and AtPRMT1b, and, furthermore, uncovered a direct interaction between the protein methyltransferase and the RNA methyltransferase. Taken together, our findings implicate AtPRMT1a and AtPRMT1b as H4-R3 protein arginine N-methyltransferases in Arabidopsis and may be involved in diverse biological processes inside and outside the nucleus.
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BOULANGER, Marie-Chloé, Tina Branscombe MIRANDA, Steven CLARKE, Marco di FRUSCIO, Beat SUTER, Paul LASKO, and Stéphane RICHARD. "Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4." Biochemical Journal 379, no. 2 (April 15, 2004): 283–89. http://dx.doi.org/10.1042/bj20031176.

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The role of arginine methylation in Drosophila melanogaster is unknown. We identified a family of nine PRMTs (protein arginine methyltransferases) by sequence homology with mammalian arginine methyltransferases, which we have named DART1 to DART9 (Drosophilaarginine methyltransferases 1–9). In keeping with the mammalian PRMT nomenclature, DART1, DART4, DART5 and DART7 are the putative homologues of PRMT1, PRMT4, PRMT5 and PRMT7. Other DART family members have a closer resemblance to PRMT1, but do not have identifiable homologues. All nine genes are expressed in Drosophila at various developmental stages. DART1 and DART4 have arginine methyltransferase activity towards substrates, including histones and RNA-binding proteins. Amino acid analysis of the methylated arginine residues confirmed that both DART1 and DART4 catalyse the formation of asymmetrical dimethylated arginine residues and they are type I arginine methyltransferases. The presence of PRMTs in D. melanogaster suggest that flies are a suitable genetic system to study arginine methylation.
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Cheung, Ngai, Li Chong Chan, Alex Thompson, Michael L. Cleary, and Chi Wai Eric So. "Protein arginine-methyltransferase-dependent oncogenesis." Nature Cell Biology 9, no. 10 (September 23, 2007): 1208–15. http://dx.doi.org/10.1038/ncb1642.

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Mowen, K. A., and M. David. "Analysis of Protein Arginine Methylation and Protein Arginine-Methyltransferase Activity." Science Signaling 2001, no. 93 (July 31, 2001): pl1. http://dx.doi.org/10.1126/stke.2001.93.pl1.

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Gou, Qing, ShuJiao He, and ZeJian Zhou. "Protein arginine N-methyltransferase 1 promotes the proliferation and metastasis of hepatocellular carcinoma cells." Tumor Biology 39, no. 2 (February 2017): 101042831769141. http://dx.doi.org/10.1177/1010428317691419.

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Hepatocellular carcinoma is the most common subtype of liver cancer. Protein arginine N-methyltransferase 1 was shown to be upregulated in various cancers. However, the role of protein arginine N-methyltransferase 1 in hepatocellular carcinoma progression remains incompletely understood. We investigated the clinical and functional significance of protein arginine N-methyltransferase 1 in a series of clinical hepatocellular carcinoma samples and a panel of hepatocellular carcinoma cell lines. We performed suppression analysis of protein arginine N-methyltransferase 1 using small interfering RNA to determine the biological roles of protein arginine N-methyltransferase 1 in hepatocellular carcinoma. In addition, the expression of epithelial-mesenchymal transition indicators was verified by western blotting in hepatocellular carcinoma cell lines after small interfering RNA treatment. Protein arginine N-methyltransferase 1 expression was found to be significantly upregulated in hepatocellular carcinoma cell lines and clinical tissues. Moreover, downregulation of protein arginine N-methyltransferase 1 in hepatocellular carcinoma cells by small interfering RNA could inhibit cell proliferation, migration, and invasion in vitro. These results indicate that protein arginine N-methyltransferase 1 may contribute to hepatocellular carcinoma progression and serves as a promising target for the treatment of hepatocellular carcinoma patients.
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Al-Hamashi, Ayad A., Krystal Diaz, and Rong Huang. "Non-Histone Arginine Methylation by Protein Arginine Methyltransferases." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 699–712. http://dx.doi.org/10.2174/1389203721666200507091952.

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Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we highlight the most recent clinical studies for several PRMT inhibitors.
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Côté, Jocelyn, Franc˛ois-Michel Boisvert, Marie-Chloé Boulanger, Mark T. Bedford, and Stéphane Richard. "Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1." Molecular Biology of the Cell 14, no. 1 (January 2003): 274–87. http://dx.doi.org/10.1091/mbc.e02-08-0484.

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RNA binding proteins often contain multiple arginine glycine repeats, a sequence that is frequently methylated by protein arginine methyltransferases. The role of this posttranslational modification in the life cycle of RNA binding proteins is not well understood. Herein, we report that Sam68, a heteronuclear ribonucleoprotein K homology domain containing RNA binding protein, associates with and is methylated in vivo by the protein arginineN-methyltransferase 1 (PRMT1). Sam68 contains asymmetrical dimethylarginines near its proline motif P3 as assessed by using a novel asymmetrical dimethylarginine-specific antibody and mass spectrometry. Deletion of the methylation sites and the use of methylase inhibitors resulted in Sam68 accumulation in the cytoplasm. Sam68 was also detected in the cytoplasm of PRMT1-deficient embryonic stem cells. Although the cellular function of Sam68 is unknown, it has been shown to export unspliced human immunodeficiency virus RNAs. Cells treated with methylase inhibitors prevented the ability of Sam68 to export unspliced human immunodeficiency virus RNAs. Other K homology domain RNA binding proteins, including SLM-1, SLM-2, QKI-5, GRP33, and heteronuclear ribonucleoprotein K were also methylated in vivo. These findings demonstrate that RNA binding proteins are in vivo substrates for PRMT1, and their methylation is essential for their proper localization and function.
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van Haren, Matthijs J., Nils Marechal, Nathalie Troffer-Charlier, Agostino Cianciulli, Gianluca Sbardella, Jean Cavarelli, and Nathaniel I. Martin. "Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1." Proceedings of the National Academy of Sciences 114, no. 14 (March 22, 2017): 3625–30. http://dx.doi.org/10.1073/pnas.1618401114.

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Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics. These constructs were found to be potent CARM1 inhibitors and also formed stable complexes with the enzyme. High-resolution crystal structures of CARM1 in complex with these compounds confirm a mode of binding that is indeed reflective of the transition state at the CARM1 active site. Given the transient nature of PRMT–substrate complexes, such transition state mimics represent valuable chemical tools for structural studies aimed at deciphering the regulation of arginine methylation mediated by the family of arginine methyltransferases.
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Gupta, Somlee, Rajashekar Varma Kadumuri, Anjali Kumari Singh, Sreenivas Chavali, and Arunkumar Dhayalan. "Structure, Activity and Function of the Protein Arginine Methyltransferase 6." Life 11, no. 9 (September 11, 2021): 951. http://dx.doi.org/10.3390/life11090951.

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Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous substrate proteins. PRMT6 introduces asymmetric dimethylation modification in the histone 3 at arginine 2 (H3R2me2a) and facilitates epigenetic regulation of global gene expression. In addition to histones, PRMT6 methylates a wide range of cellular proteins and regulates their functions. Here, we discuss (i) the biochemical aspects of enzyme kinetics, (ii) the structural features of PRMT6 and (iii) the diverse functional outcomes of PRMT6 mediated arginine methylation. Finally, we highlight how dysregulation of PRMT6 is implicated in various types of cancers and response to viral infections.
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Cha, Boksik, Yaerin Park, Byul Nim Hwang, So-young Kim, and Eek-hoon Jho. "Protein Arginine Methyltransferase 1 Methylates Smurf2." Molecules and Cells 38, no. 8 (July 1, 2015): 723–28. http://dx.doi.org/10.14348/molcells.2015.0113.

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Dissertations / Theses on the topic "Protein arginine methyltransferase"

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Zamiri, Maryam. "Synthesis of protein arginine N-methyltransferase 6 inhibitors." Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/43808.

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Protein arginine N-methyltransferases (PRMTs) are pertinent targets for drug discovery as their dysfunction is associated with a number of diseases such as cancers, cardiovascular diseases and viral pathogenesis. The precise role of PRMTs in the initiation, development, or progression of diseases is not known yet. Due to association of PRMT1 and 4 with transcriptional activation, the main focus of inhibitor discovery has been on these two enzymes. On the other hand, the goal of this study is to find a PRMT6 specific inhibitor. PRMT6 methylates DNA polymerase β, histones H3 and H4 and HIV proteins: Rev and Tat. PRMT6 uses S-adenosyl-L-methionine (AdoMet) as the “methyl group” source. AdoMet fits into a distinct conserved binding site in the enzyme, which is located adjacent to the protein substrate/catalytic site such that its S⁺-Me motif is correctly positioned with respect to the substrate arginine nitrogen atom that undergoes methylation. Based on crystallography data for PRMT1, the purine C8 center in AdoMet is in close proximity to the methionine sulfur atom (M166 in PRMT6). As shown by Frankel et al. (Faculty of Pharmaceutical Sciences, UBC), the M166C PRMT6 mutant displays activity. Based upon this observation, we hypothesize that Ado-Met analogues with reactive substituents (e.g., CHO) at C8 position of adenine ring will form a covalent bond with the proximal Cys SH group in M166C PRMT6. This validates our further hypothesize that in appropriately designed analogues, it will be possible to subsequently detach the sugar and amino acid components of Ado-Met to leave the adenine ring component alone bound to the enzyme. This provides a unique opportunity to explore the “fragment based approach in drug discovery” to design PRMT6 specific inhibitors.
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Hong, Wei. "Design and synthesis of protein arginine methyltransferase inhibitors." Thesis, University of Nottingham, 2010. http://eprints.nottingham.ac.uk/12835/.

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Biological methylation is defined as the transfer of a methyl group from S-adenosyl-L-methionine(SAM) to one of a wide range of potential acceptors such as DNA, RNA, protein, hormones and neurotransmitters. Protein arginine methylation is a common post-translational modification facilitated by protein arginine methyltransferases(e.g. PRMTI). The roles of these enzymes in vivo are currently poorly understood. The focus of the project is design and synthesis of PRMT inhibitors with the ultimate goal of evaluating their activities in cells. Preliminary work toward the synthesis of S-adenosyl-trifluoromethyl-L-homocystein and adenosyl 5'-[2-(tert-butoxycarbonylamino)ethyl-trifluoro methyl] thiophenium is described. The ternary crystal structure of PRMTI in complex with S-adenoSyl-L-homocystein(eSAH) and an arginine containing peptide (PBD IOR8) was used to design a series of potential bisubstrate inhibitors of PRMTI. The prototypical SAM analogues bearing guanidine group were sought to replace the reactive sulfonium centre with nitrogen. Analogue synthesis proceeded via successive reductive arnination of Y-arnino-Y-deoxyadenosine and deprotection in good overall yields. An alkyne SAM analogue, 5'-[(S-3-amino-3-carboxypropyl)-propargylaminol-5'-deoxyadenosine was prepared, which underwent efficient Cu(1) catalysed Huisgen reaction to yield a triazole derived SAM analogue 5'-[(S-3-amino-3-carboxypropyl)-[I-(2-guanidinoethyl)-IH-1,2,3-triazol-4-yl]methyl-amino]-5'-deoxyadenosine. Preliminary biological evaluation of the compounds by collaborators Professor Steve Ward and Dr Richard Parry at the University of Bath, confirmed that 5'-[(S-3-amino-3-carboxypropyl)- 3-guanidinopropyl-amino]-5'-deoxyadenosine and 5-[(S-3-amino-3-carboxypropyl)-5-guanidinopentyl-amino]-5'-deoxyadenosine are potent inhibitors of PRMTI but not the lysine methyltransferase SET7. A related N-6 modified SAM analogue 5'-[(S-3-amino-3-carboxypropyl)-3-guanidinopropylamino]-5'-deoxy-N6-(lI-azido-3,6,9-trioxaundecane)-amino adenosine bearing an azide tether was developed with the aim of allowing facile introduction of biotin or fluorescent dyes, using either Staudinger ligation, or Cu(1) catalysed Huisgen reaction to provide compounds that can be used for affinity purification of the target protein or study of its localisation in cells respectively. Finally, progress toward a novel, rapid and enantioselective synthesis of the natural product (+)-sinefungin is reported. Key dihydropyridazine intermediates were generated from adenosyl 5'-propaldehyde, commercially available azodicarboxylate derivatives and ester substituted vinyltriphenylphosphonium salt by successful extension of methodology first reported by Ley and co-workers. Deprotection and ring opening of clihydropyridazine compounds was attempted, and unfortunately we were not able to generate (+)-sinefungin, although it is hoped that this route can be developed to achieve this in the future.
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Pak, Laam. "Insights into a heteromeric protein arginine N-methyltransferase complex." Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/42123.

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Protein arginine N-methyltransferases (PRMTs) act in signaling pathways and gene expression by methylating arginine residues within target proteins. PRMT1 is responsible for most cellular arginine methylation activity and can work independently or in collaboration with other PRMTs. In this Ph.D. thesis I demonstrated an interaction between PRMT1 and -2 using co-immunoprecipitation and bimolecular fluorescence complementation (BiFC). As a result of this interaction, PRMT2 stimulated PRMT1 methyltransferase activity, affecting its apparent Vmax and Km values in vitro, and increasing the production of methylarginines in cells. Active site mutations and regional deletions on PRMT1 and -2 were also investigated, which demonstrated that complex formation required full-length, active PRMT1. However, the interaction between PRMT1 and -2 proved insensitive to methylation inhibition in the absence of the PRMT2 Src homology 3 (SH3) domain, which suggests that the PRMT2 SH3 domain may mediate this interaction between PRMT1 and -2 in a methylation-dependent fashion. The role of the PRMT2 SH3 domain was investigated through screening for its associated proteins using GST-pull down assays followed by LC-MS/MS proteomic analysis. The result of this study revealed associations of the PRMT2 SH3 domain with at least 29 splicing-related proteins, suggesting a potential role of PRMT2 in regulating pre-mRNA processing and splicing. The interaction between PRMT2 and the Src substrate associated in mitosis of 68 kDa (Sam68) possibly through the PRMT2 SH3 domain was demonstrated using co-immunoprecipitation. Additionally, immunofluorescence results present herein imply that the PRMT2 SH3 domain could affect Sam68 sub-cellular localization in hypomethylated HeLa cells. The biological functions of PRMT2 and the PRMT1/2 heteromeric complex were explored by pursuing the identity of associated proteins common to both PRMT1 and -2 using mass spectrometry proteomics. Approximately 50% of the identified protein hits have reported roles in controlling gene expression, while other hits are involved in diverse cellular processes such as protein folding, degradation, and metabolism. Importantly, three novel PRMT2 binders, p53, promyelocytic leukemia protein (PML), and extra eleven nineteen (EEN) were uncovered, suggesting that PRMT2 could participate in regulation of transcription and apoptosis through PRMT2-protein interactions.
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Smith, Porsha L. "Protein Arginine Methyltransferase 5 as a Driver of Lymphomagenesis." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1468975682.

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May, Kyle M. "Investigation of Protein Dynamics and Communication in Adomet-Dependent Methyltransferases: Non-Ribosomal Peptide Synthetase and Protein Arginine Methyltransferase." DigitalCommons@USU, 2019. https://digitalcommons.usu.edu/etd/7550.

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For many enzymes to function correctly they must have the freedom to display a level of dynamics or communication during their catalytic cycle. The effects that protein dynamics and communication can have are wide ranging, from changes in substrate specificity or product profiles, to speed of reaction or switching activity on or off. This project investigates the protein dynamics and communication in two separate systems, a non-ribosomal peptide synthetase (NRPS), and a protein arginine methyltransferase (PRMT). PRMT1, the enzyme responsible for 80% of arginine methylation in humans, has been implicated in a variety of disease states when functioning incorrectly. For this reason, much focus has been placed on better understanding how PRMT1 determines which products it creates and at what times. This project aims to shed light on how dynamics and communication within PRMT1 dictate its activity. We have to this point developed a protocol for creating and purifying a linked PRMT1 construct which will enable us to conduct the necessary experiments capable of answering our larger questions about the PRMT1 catalytic mechanism. Our collaborators in the Zhan lab discovered the presence of a methyltransferase (Mt) in the two NRPS systems they study, which produce two different and medically relevant compounds, bassianolide and beauvericin. The Hevel lab is well suited to study methyltransferases and so were asked to help evaluate the role of these Mt domains and how they affect the production of the relevant natural products. Achieving a more complete understanding of these systems will move us closer toward the “holy grail” of being able to manipulate and harness NRPS systems for the engineering of novel medically relevant compounds. This project has found that the Mt domain substrate specificity is affected by the surrounding protein domains, or even small portions of them.
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Feng, You. "Kinetic Mechanism and Inhibitory Study of Protein Arginine Methyltransferase 1." Digital Archive @ GSU, 2012. http://digitalarchive.gsu.edu/chemistry_diss/68.

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Protein arginine methyltransferase 1 (PRMT1) is a key posttranslational modification enzyme that catalyzes the methylation of specific arginine residues in histone and nonhistone protein substrates, regulating diverse cellular processes such as transcriptional initiation, RNA splicing, DNA repair, and signal transduction. Recently the essential roles of PRMT1 in cancer and cardiovascular complications have intrigued much attention. Developing effective PRMT inhibitors therefore is of significant therapeutic value. The research on PRMT inhibitor development however is greatly hindered by poor understanding of the biochemical basis of protein arginine methylation and lack of effective assays for PRMT1 inhibitor screening. Herein, we report our effort in the kinetic mechanism study as well as the fluorescent probe and inhibitor development for PRMT1. New fluorescent reporters were designed and applied to perform single-step analysis of substrate binding and methylation of PRMT1. Using these reporters, we performed transient-state fluorescence measurements to dissect the rate constants along the PRMT1 catalytic coordinate. The data give evidence that the chemistry of methyl transfer is the major rate-limiting step, and that binding of the cofactor SAM or SAH affects the association and dissociation of H4 with PRMT1. Importantly, we identified a critical kinetic step suggesting a precatalytic conformational transition induced by substrate binding. On the other hand, we discovered a type of naphthyl-sulfo (NS) compounds that block PRMT1- mediated arginine methylation at micromolar potency through a unique mechanism: they directly target the substrates but not PRMT enzymes for the observed inhibition. We also found that suramin, an anti-parasite and anti-cancer drug bearing similar functional groups, effectively inhibited PRMT1 mediated methylation. These findings about novel PRMT inhibitors and their unique inhibition mechanism provide a new way for chemical regulation of protein arginine methylation. Addionally, to dissect the interplaying relationship between different histone modification marks, we investigated how individual lysine acetylations and their different combinations at the H4 tail affect Arg-3 methylation in cis. Our data reveal that the effect of lysine acetylation on arginine methylation depends on the site of acetylation and the type of methylation. While certain acetylations present a repressive impact on PRMT-1 mediated methylation (type I methylation), lysine acetylation generally is correlated with enhanced methylation by PRMT5 (type II dimethylation). In particular, Lys-5 acetylation decreases activity of PRMT1 but increases that of PRMT5. Furthermore, hyperacetylation increases the content of ordered secondary structures of H4 tail. These findings provide new insights into the regulatory mechanism of Arg-3 methylation by H4 acetylation, and unravel that complex intercommunications exist between different posttranslational marks in cis.
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Pelletier, Marie-Eve. "PRMT8: Characterization of a novel neuron-specific protein arginine methyltransferase." Thesis, University of Ottawa (Canada), 2010. http://hdl.handle.net/10393/28467.

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Methylation of arginine residues is a post-translational modification mediated by specific enzymes known as the Protein Arginine Methyltransferase (PRMT) family. In this thesis, we present our research on PRMT8, an enzyme catalyzing the formation of asymmetric dimethylarginine (aDMA), which displays a unique distribution at the plasma membrane of neuronal cells of the central nervous system (CNS). An ontogenic analysis of PRMT8 in mouse tissues revealed that its expression in the brain is induced during the perinatal stage and is maintained in adulthood. The P19 cell line was identified as a valid model for endogenous PRMT8 and showed the induction and requirement of PRMT8 to achieve neuronal processes. A P19 PRMT8 knock-down cell line does not survive neuronal differentiation while, in contrast, no cell death is observed when the muscle lineage is induced. Taken together, these findings suggest an important role for PRMT8 in neuronal differentiation and/or function in the CNS.
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Morales, Yalemi. "Characterization of the Substrate Interactions and Regulation of Protein Arginine Methyltransferase." DigitalCommons@USU, 2016. https://digitalcommons.usu.edu/etd/5074.

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Protein arginine methylation is a posttranslational modification catalyzed by the family of proteins known as the protein arginine methyltransferases (PRMTs). Thousands of methylated arginines have been found in mammalian cells. Many targets of arginine regulation are involved in important cellular processes like transcription, RNA transport and processing, translation, cellular signaling, and DNA repair. Since PRMT dysregulation has been linked to a variety of disease states, understanding how the activity of the PRMTs is regulated is of paramount importance. PRMT1 is the predominant PRMT, responsible for about 85% of all arginine methylation in cells, but very little is known about how PRMT1 is regulated. Although a few methods to regulate PRMT1 activity have been reported, the details of interaction and regulatory mechanisms remain largely unknown. To better understand how PRMT1 is able to bind its substrates and how PRMT1 activity is regulated, we followed a mechanistic and structural biology approach to better understand how PRMT1 interacts with its substrates and protein regulators. In this study the regulation of Hmt1 methyltransferase activity by the Air1 and Air2 proteins was analyzed and only one was determined to affect Hmt1 activity. The posttranslational phosphorylation of Hmt1 had also been reported to affect Hmt1 activity in vivo and our preliminary studies suggest that additional factors may help influence the regulatory effect of phosphorylation. Lastly, we report a new method of PRMT regulation through the reversible oxidation of key PRMT1 cysteine residues. We are also able to show that this regulation occurs in cells and affects several PRMT isoforms.
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Dacwag, Caroline S. "Analysis of Protein Arginine Methyltransferase Function during Myogenic Gene Transcription: A Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/402.

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Skeletal muscle differentiation requires synergy between tissue-specific transcription factors, chromatin remodeling enzymes and the general transcription machinery. Here we demonstrate that two distinct protein arginine methyltransferases are required to complete the differentiation program. Prmt5 is a type II methyltransferase, symmetrically dimethylates histones H3 and H4 and has been shown to play a role in transcriptional repression. An additional member of the Prmt family, Carm1 is a type I methyltransferase, and asymmetrically methylates histone H3 and its substrate proteins. MyoD regulates the activation of the early class of skeletal muscle genes, which includes myogenin. Prmt5 was bound to and dimethylates H3R8 at the myogenin promoter in a differentiation-dependent fashion. When proteins levels of Prmt5 were reduced by antisense, disappearance of H3R8 dimethylation and Prmt5 binding was observed. Furthermore, binding of Brg1 to regulatory sequences of the myogenin promoter was abolished. All subsequent events relying on Brg1 function, such as chromatin remodeling and stable binding by muscle specific transcription factors such as MyoD, were eliminated. Robust association of Prmt5 and dimethylation of H3R8 at myogenin promoter sequences was observed in mouse satellite cells, the precursors of mature myofibers. Prmt5 binding and histone modification were observed to a lesser degree in mature myofibers. Therefore, these results indicate that Prmt5 is required for dimethylating histone at the myogenin locus during skeletal muscle differentiation in order to facilitate the binding of Brg1, the ATPase subunit of the chromatin remodeling complex SWI/SNF. Further exploration of the role of Prmt5 during the activation of the late class of muscle genes revealed that though Prmt5 is associated with and dimethylates histones at the regulatory elements of late muscle genes in tissue and in culture, it was dispensable for late gene activation. Previous reports had indicated that Carm1 was involved during late gene activation. We observed that Carm1 was bound to and responsible for dimethylating histones at late muscle gene promoters in tissue and in culture. In contrast to Prmt5, a complete knockout of Carm1 resulted in abrogation of late muscle gene activation. Furthermore, loss of Carm1 binding and dimethylated histones resulted in a disappearance of Brg1 binding and chromatin remodeling at late muscle gene loci. Time course chromatin immunoprecipitations revealed that Carm1 binding and histone dimethylation occurred concurrently with the onset of late gene activation. In vitro binding assays revealed that an interaction between Carm1, myogenin and Mef2D exists. These results demonstrate that Carm1 is recruited to the regulatory sequences of late muscle genes via its interaction with either myogenin or Mef2D and is responsible for dimethylates histones in order to facilitate the binding of Brg1. Therefore, these results indicate that during skeletal muscle differentiation, distinct roles exist for these Prmts such that Prmt5 is required for activation of early genes while Carm1 is essential for late gene induction.
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Haghandish, Nasim. "Characterizing the Role of Protein Arginine Methyltransferase 7 (PRMT7) in Breast Cancer." Thesis, Université d'Ottawa / University of Ottawa, 2019. http://hdl.handle.net/10393/38672.

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The development of more efficient therapeutic strategies in the treatment of breast cancer relies on understanding the biological events that promote its progression. Protein arginine methyltransferases (PRMTs) are enzymes that catalyze the methylation of arginine residues within proteins resulting in changes in several biological processes. PRMTs have been shown to be aberrantly expressed in many cancers and promote tumourigenesis and cancer progression. Specifically, PRMT7 mRNA expression correlates with breast cancer aggressiveness and invasiveness. Thus, we sought to determine whether PRMT7 promotes breast cancer progression/tumourigenesis and to further identify the functional mechanisms through which this is possible. We have shown that PRMT7 is upregulated in both breast cancer tissues and cell lines. Moreover, we have shown both in vitro and in vivo that PRMT7 enhances breast cancer cell invasion and metastasis. Using biochemical experimentation, we demonstrated that PRMT7 induces the expression of matrix metalloproteinase 9 to promote invasion and subsequent metastasis. Furthermore, using proteomic experiments, we discovered many novel PRMT7-interacting proteins. Further biochemical experimentation identified eukaryotic translation initiation factor eIF2α as an interacting protein and substrate of PRMT7. We demonstrated a regulatory interplay between eIF2α methylation and phosphorylation upon cellular stress: methylation is required for S51 phosphorylation. Accordingly, we have shown that stress granule formation, in the face of cellular stresses, was significantly diminished in PRMT7-knockdown cells. We additionally found that PRMT7 plays a regulatory role in protein translation. Overall, these findings suggest that PRMT7 plays a critical role in promoting breast cancer cell invasion, metastasis, stress regulation, and protein translation.
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Book chapters on the topic "Protein arginine methyltransferase"

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Schomburg, Dietmar, and Dörte Stephan. "Protein-arginine N-methyltransferase." In Enzyme Handbook 11, 101–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_23.

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Zou, Jin, Wei Shen, Yu Zhang, and Shibo Ying. "The Role of Protein Arginine Methyltransferase 1 in Gastrointestinal Cancers." In Post-Translational Modifications in Cellular Functions and Diseases. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96197.

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Mammals can produce nine kinds of arginine methylation enzymes that can be divided into three types (I, II, and III) according to their catalytic activity. Arginine methyltransferase 1 (PRMT1), as the first discovered arginine methyltransferase type I, has been reported to be involved in cell signal transduction, DNA damage repair, RNA transcription and other processes. Its imbalance or abnormal expression is also involved in cancer metastasis. PRMT1 is highly expressed in gastrointestinal tumors and promotes tumor biomarkers expression, chemotherapy resistance and tumorigenicity to promote cancer progression, while downregulation of PRMT1 expression can inhibit the migration and invasion of related tumor cells or promote tumor cells apoptosis and inhibit the progression of cancer. Therefore, PRMT1 may be a cancer therapeutic target. In this paper, arginine methylase 1 expression in various types of gastrointestinal tumors, the tumorigenic mechanism and the role of PRMT1 in tumorigenesis and development were reviewed.
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Qian, Kun, and Y. George Zheng. "Current Development of Protein Arginine Methyltransferase Inhibitors." In Epi-Informatics, 231–56. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-802808-7.00008-3.

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Zhang, Xing, and Xiaodong Cheng. "4 Structure of protein arginine methyltransferases." In Protein Methyltransferases, 105–21. Elsevier, 2006. http://dx.doi.org/10.1016/s1874-6047(06)80006-5.

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Bedford, Mark T. "2 The family of protein arginine metkyltransferases." In Protein Methyltransferases, 31–50. Elsevier, 2006. http://dx.doi.org/10.1016/s1874-6047(06)80004-1.

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McBride, Anne E. "3 Diverse roles of protein arginine methyltransferases." In Protein Methyltransferases, 51–103. Elsevier, 2006. http://dx.doi.org/10.1016/s1874-6047(06)80005-3.

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Kuhn, Peter, and Wei Xu. "Chapter 9 Protein Arginine Methyltransferases." In Progress in Molecular Biology and Translational Science, 299–342. Elsevier, 2009. http://dx.doi.org/10.1016/s1877-1173(09)87009-9.

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Conference papers on the topic "Protein arginine methyltransferase"

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Zou, C., Y. Lai, and X. Li. "The Role of Protein Arginine Methyltransferase PRMT4 in Septic Immunosuppression." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a7066.

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Zhou, Xin. "Molecular Dynamics Simulation and Free Energy Calculation of Protein Arginine Methyltransferase 1." In 2nd International Conference on Material Science, Energy and Environmental Engineering (MSEEE 2018). Paris, France: Atlantis Press, 2018. http://dx.doi.org/10.2991/mseee-18.2018.27.

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Yildirim, Ali O., Melanie Konigshoff, Qiongman Wang, and Oliver Eickelberg. "Expression Profiling Of Protein Arginine Methyltransferase (Prmt) Isoforms In Chronic Obstructive Pulmonary Disease (COPD)." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4954.

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Sun, Qingzhu, Daiana Stolz, Michael Tamm, Shemin Lu, and Michael Roth. "Characterizations and potential functions of protein arginine methyltransferase 1 in primary lung structural cells." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa3882.

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Yan, Fengting, Lapo Alinari, Mark Lustberg, L. Katherine Martin, Oskar Nowicki, Xin Wu, Bo Yu, et al. "Abstract 1584: Targeting protein arginine methyltransferase 5 (PRMT5) enzyme over expression in high grade astrocytomas." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1584.

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Silvestre, David, Amélie Brisson, Bérengère Marty-Prouvost, Mengliang Ye, Hélène Bonsang, Virginie Maire, Damarys Loew, et al. "Abstract 3809: Protein arginine methyltransferase 1 (PRMT1) is a candidate therapeutic target for breast cancers." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3809.

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Shifteh, David, Tzuriel Sapir, Sanjay Goel, and Radhashree Maitra. "Abstract 2916: Protein arginine methyltransferase 5 as a therapeutic target for KRAS mutated colorectal cancer." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-2916.

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Chan, LH, L. Zhou, Kai Yu Ng, TL Wong, TK Lee, YP Ching, YF Yuan, et al. "Abstract 4479: Protein arginine methyltransferase PRMT6 regulates cancer stemness through CRAF methylation in hepatocellular carcinoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4479.

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Chikkanna, Dinesh, Sunil Kumar Panigrahi, Sujatha Rajagopalan, Srinivasa Raju Sammeta, Anirudha Lakshminarasimhan, Mohan R, Narasihmarao K, et al. "Abstract A174: Novel inhibitors of protein arginine methyltransferase 5 (PRMT5) for the treatment of solid tumors." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; October 26-30, 2017; Philadelphia, PA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1535-7163.targ-17-a174.

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Shaw, Vikram, Yuji Piao, Soon Young Park, Jianwen Dong, Emmanuel Martinez-Ledesma, Caroline Carrillo, Verlene Henry, et al. "Abstract 4858: Efficacy of the protein arginine methyltransferase PRMT5 inhibitor GSK591 in glioma stem-like cells." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4858.

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