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Journal articles on the topic 'Protein arginine methyltransferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

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 (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 (H4

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2

BOULANGER, Marie-Chloé, Tina Branscombe MIRANDA, Steven CLARKE, et al. "Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4." Biochemical Journal 379, no. 2 (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 developmen

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3

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 (2007): 1208–15. http://dx.doi.org/10.1038/ncb1642.

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4

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

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5

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 (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

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6

Al-Hamashi, Ayad A., Krystal Diaz, and Rong Huang. "Non-Histone Arginine Methylation by Protein Arginine Methyltransferases." Current Protein & Peptide Science 21, no. 7 (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 high

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7

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 (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 dimethylarg

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8

van Haren, Matthijs J., Nils Marechal, Nathalie Troffer-Charlier, et al. "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 (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 comple

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9

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 (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 di

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10

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 (2015): 723–28. http://dx.doi.org/10.14348/molcells.2015.0113.

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11

Li, Hong-Tao, Ting Gong, Zhen Zhou, et al. "Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro." Biochemical Journal 467, no. 3 (2015): 507–15. http://dx.doi.org/10.1042/bj20141437.

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Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs’ substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT and methylates histone H4 arginine 3 and several mRNA-binding proteins. Hmt1 forms dimers or oligomers, but how dimerization or oligomerization affects its activity remains largely unknown. We now report that Hmt1 can methylate histone H3 arginine 2 (H3R2) in vitro. The dimerization but not hexamerization is essential for Hmt1’s activity. Interestin

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12

RICHARD, Stéphane, Mélanie MOREL, and Patrick CLÉROUX. "Arginine methylation regulates IL-2 gene expression: a role for protein arginine methyltransferase 5 (PRMT5)." Biochemical Journal 388, no. 1 (2005): 379–86. http://dx.doi.org/10.1042/bj20040373.

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Arginine methylation is a post-translational modification resulting in the generation of aDMAs (asymmetrical ω-NG, NG-dimethylated arginines) and sDMAs (symmetrical ω-NG, N′G-dimethylated arginines). The role of arginine methylation in cell signalling and gene expression in T lymphocytes is not understood. In the present study, we report a role for protein arginine methylation in regulating IL-2 (interleukin 2) gene expression in T lymphocytes. Leukaemic Jurkat T-cells treated with a known methylase inhibitor, 5′-methylthioadenosine, had decreased cytokine gene expression, as measured using an

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13

Gou, Y., J. Li, O. Jackson-Weaver, et al. "Protein Arginine Methyltransferase PRMT1 Is Essential for Palatogenesis." Journal of Dental Research 97, no. 13 (2018): 1510–18. http://dx.doi.org/10.1177/0022034518785164.

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Cleft palate is among the most common birth defects. Currently, only 30% of cases have identified genetic causes, whereas the etiology of the majority remains to be discovered. We identified a new regulator of palate development, protein arginine methyltransferase 1 (PRMT1), and demonstrated that disruption of PRMT1 function in neural crest cells caused complete cleft palate and craniofacial malformations. PRMT1 is the most highly expressed of the protein arginine methyltransferases, enzymes responsible for methylation of arginine motifs on histone and nonhistone proteins. PRMT1 regulates sign

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14

Gao, Wei-wei, Rong-quan Xiao, Bing-ling Peng та ін. "Arginine methylation of HSP70 regulates retinoid acid-mediated RARβ2 gene activation". Proceedings of the National Academy of Sciences 112, № 26 (2015): E3327—E3336. http://dx.doi.org/10.1073/pnas.1509658112.

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Although “histone” methyltransferases and demethylases are well established to regulate transcriptional programs and to use nonhistone proteins as substrates, their possible roles in regulation of heat-shock proteins in the nucleus have not been investigated. Here, we report that a highly conserved arginine residue, R469, in HSP70 (heat-shock protein of 70 kDa) proteins, an evolutionarily conserved protein family of ATP-dependent molecular chaperone, was monomethylated (me1), at least partially, by coactivator-associated arginine methyltransferase 1/protein arginine methyltransferase 4 (CARM1/

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15

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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16

Tan, Choon Ping, and Sara Nakielny. "Control of the DNA Methylation System Component MBD2 by Protein Arginine Methylation." Molecular and Cellular Biology 26, no. 19 (2006): 7224–35. http://dx.doi.org/10.1128/mcb.00473-06.

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ABSTRACT DNA methylation is vital for proper chromatin structure and function in mammalian cells. Genetic removal of the enzymes that catalyze DNA methylation results in defective imprinting, transposon silencing, X chromosome dosage compensation, and genome stability. This epigenetic modification is interpreted by methyl-DNA binding domain (MBD) proteins. MBD proteins respond to methylated DNA by recruiting histone deacetylases (HDAC) and other transcription repression factors to the chromatin. The MBD2 protein is dispensable for animal viability, but it is implicated in the genesis of colon

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17

Boulanger, Marie-Chloé, Chen Liang, Rodney S. Russell, et al. "Methylation of Tat by PRMT6 Regulates Human Immunodeficiency Virus Type 1 Gene Expression." Journal of Virology 79, no. 1 (2005): 124–31. http://dx.doi.org/10.1128/jvi.79.1.124-131.2005.

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ABSTRACT The human immunodeficiency virus (HIV) transactivator protein, Tat, stimulates transcription from the viral long terminal repeats via an arginine-rich transactivating domain. Since arginines are often known to be methylated, we investigated whether HIV type 1 (HIV-1) Tat was a substrate for known protein arginine methyltransferases (PRMTs). Here we identify Tat as a substrate for the arginine methyltransferase, PRMT6. Tat is specifically associated with and methylated by PRMT6 within cells. Overexpression of wild-type PRMT6, but not a methylase-inactive PRMT6 mutant, decreased Tat tra

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18

KZHYSHKOWSKA, Julia, Elisabeth KREMMER, Markus HOFMANN, Hans WOLF, and Thomas DOBNER. "Protein arginine methylation during lytic adenovirus infection." Biochemical Journal 383, no. 2 (2004): 259–65. http://dx.doi.org/10.1042/bj20040210.

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Arginine methylation of proteins affects major processes in the cell, including transcriptional regulation, mRNA metabolism, signal transduction and protein sorting. Arginine methylation of Ad (adenovirus) E1B 55-kDa-associated protein E1B-AP5 was recently described by us [Kzhyshkowska, Schutt, Liss, Kremmer, Stauber, Wolf and Dobner (2001) Biochem. J. 358, 305–314]. In this first example of protein arginine methylation analysis in Ad-infected cells, we investigated methylation of the E1B-AP5 and the viral L4-100 kDa protein. We demonstrate that E1B-AP5 methylation is enhanced during the cours

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19

Richters, André. "Targeting protein arginine methyltransferase 5 in disease." Future Medicinal Chemistry 9, no. 17 (2017): 2081–98. http://dx.doi.org/10.4155/fmc-2017-0089.

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20

Obianyo, Obiamaka, Tanesha C. Osborne, and Paul R. Thompson. "Kinetic Mechanism of Protein Arginine Methyltransferase 1†." Biochemistry 47, no. 39 (2008): 10420–27. http://dx.doi.org/10.1021/bi800904m.

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21

Gary, Jonathan D., Wey-Jinq Lin, Melody C. Yang, Harvey R. Herschman, and Steven Clarke. "The Predominant Protein-arginine Methyltransferase fromSaccharomyces cerevisiae." Journal of Biological Chemistry 271, no. 21 (1996): 12585–94. http://dx.doi.org/10.1074/jbc.271.21.12585.

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22

Lin, Hong, and Juan I. Luengo. "Nucleoside protein arginine methyltransferase 5 (PRMT5) inhibitors." Bioorganic & Medicinal Chemistry Letters 29, no. 11 (2019): 1264–69. http://dx.doi.org/10.1016/j.bmcl.2019.03.042.

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23

Woodsmith, Jonathan, Victoria Casado-Medrano, Nouhad Benlasfer, et al. "Interaction modulation through arrays of clustered methyl-arginine protein modifications." Life Science Alliance 1, no. 5 (2018): e201800178. http://dx.doi.org/10.26508/lsa.201800178.

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Systematic analysis of human arginine methylation identifies two distinct signaling modes; either isolated modifications akin to canonical post-translational modification regulation, or clustered arrays within disordered protein sequence. Hundreds of proteins contain these methyl-arginine arrays and are more prone to accumulate mutations and more tightly expression-regulated than dispersed methylation targets. Arginines within an array in the highly methylated RNA-binding protein synaptotagmin binding cytoplasmic RNA interacting protein (SYNCRIP) were experimentally shown to function in concer

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24

Janisiak, Joanna, Patrycja Kopytko, and Maciej Tarnowski. "Dysregulation of protein argininemethyltransferase in the pathogenesis of cancerpy." Postępy Higieny i Medycyny Doświadczalnej 75 (April 27, 2021): 272–82. http://dx.doi.org/10.5604/01.3001.0014.8521.

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Arginine methylation is considered to be one of the most permanent and one of the most frequent post-translational modifications. The reaction of transferring a methyl group from S-adenosylmethionine to arginine residue is catalyzed by aginine methyltransferase (PRMT). In humans there are nine members of the PRMT family, named in order of discovery of PRMT1- PRMT9. Arginine methyltransferases were divided into three classes: I, II, III, with regard to the product of the catalyzed reaction. The products of their activity are, respectively, the following: asymmetric dimethylarginine (ADMA), symm

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25

Obianyo, Obiamaka, Corey P. Causey, Justin E. Jones, and Paul R. Thompson. "Activity-Based Protein Profiling of Protein Arginine Methyltransferase 1." ACS Chemical Biology 6, no. 10 (2011): 1127–35. http://dx.doi.org/10.1021/cb2001473.

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26

Dacwag, Caroline S., Mark T. Bedford, Saïd Sif, and Anthony N. Imbalzano. "Distinct Protein Arginine Methyltransferases Promote ATP-Dependent Chromatin Remodeling Function at Different Stages of Skeletal Muscle Differentiation." Molecular and Cellular Biology 29, no. 7 (2009): 1909–21. http://dx.doi.org/10.1128/mcb.00742-08.

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ABSTRACT Temporal regulation of gene expression is a hallmark of cellular differentiation pathways, yet the mechanisms controlling the timing of expression for different classes of differentiation-specific genes are not well understood. We previously demonstrated that the class II arginine methyltransferase Prmt5 was required for skeletal muscle differentiation at the early stages of myogenesis (C. S. Dacwag, Y. Ohkawa, S. Pal, S. Sif, and A. N. Imbalzano, Mol. Cell. Biol. 27:384-394, 2007). Specifically, when Prmt5 levels were reduced, the ATP-dependent SWI/SNF chromatin-remodeling enzymes co

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27

Zhang, Meifeng, Wei Wu, Ming Gao, et al. "Coactivator-associated arginine methyltransferase 1 promotes cell growth and is targeted by microRNA-195-5p in human colorectal cancer." Tumor Biology 39, no. 3 (2017): 101042831769430. http://dx.doi.org/10.1177/1010428317694305.

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The pathogenesis of colorectal cancer remains poorly understood. Here, we show that coactivator-associated arginine methyltransferase 1 is frequently upregulated in colorectal cancer tissues and promotes cell growth in vitro and in vivo. Using bioinformatics-based prediction and luciferase reporter system, we found that coactivator-associated arginine methyltransferase 1 is post-transcriptionally targeted by microRNA-195-5p in colorectal cancer. Ectopic expression of microRNA-195-5p led to the suppression of the coactivator-associated arginine methyltransferase 1 3′-untranslated regions activi

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28

Debler, Erik W., Kanishk Jain, Rebeccah A. Warmack, et al. "A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase." Proceedings of the National Academy of Sciences 113, no. 8 (2016): 2068–73. http://dx.doi.org/10.1073/pnas.1525783113.

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Trypanosoma brucei PRMT7 (TbPRMT7) is a protein arginine methyltransferase (PRMT) that strictly monomethylates various substrates, thus classifying it as a type III PRMT. However, the molecular basis of its unique product specificity has remained elusive. Here, we present the structure of TbPRMT7 in complex with its cofactor product S-adenosyl-l-homocysteine (AdoHcy) at 2.8 Å resolution and identify a glutamate residue critical for its monomethylation behavior. TbPRMT7 comprises the conserved methyltransferase and β-barrel domains, an N-terminal extension, and a dimerization arm. The active si

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29

Wu, Christine C., Michael J. MacCoss, Gonzalo Mardones, et al. "Organellar Proteomics Reveals Golgi Arginine Dimethylation." Molecular Biology of the Cell 15, no. 6 (2004): 2907–19. http://dx.doi.org/10.1091/mbc.e04-02-0101.

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The Golgi complex functions to posttranslationally modify newly synthesized proteins and lipids and to sort them to their sites of function. In this study, a stacked Golgi fraction was isolated by classical cell fractionation, and the protein complement (the Golgi proteome) was characterized using multidimensional protein identification technology. Many of the proteins identified are known residents of the Golgi, and 64% of these are predicted transmembrane proteins. Proteins localized to other organelles also were identified, strengthening reports of functional interfacing between the Golgi a

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30

Cook, Jeffry R., Jin-Hyung Lee, Zhi-Hong Yang, et al. "FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues." Biochemical and Biophysical Research Communications 342, no. 2 (2006): 472–81. http://dx.doi.org/10.1016/j.bbrc.2006.01.167.

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31

Gonsalvez, Graydon B., Liping Tian, Jason K. Ospina, François-Michel Boisvert, Angus I. Lamond, and A. Gregory Matera. "Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins." Journal of Cell Biology 178, no. 5 (2007): 733–40. http://dx.doi.org/10.1083/jcb.200702147.

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Small nuclear ribonucleoproteins (snRNPs) are core components of the spliceosome. The U1, U2, U4, and U5 snRNPs each contain a common set of seven Sm proteins. Three of these Sm proteins are posttranslationally modified to contain symmetric dimethylarginine (sDMA) residues within their C-terminal tails. However, the precise function of this modification in the snRNP biogenesis pathway is unclear. Several lines of evidence suggest that the methyltransferase protein arginine methyltransferase 5 (PRMT5) is responsible for sDMA modification of Sm proteins. We found that in human cells, PRMT5 and a

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32

Halabelian, Levon, and Dalia Barsyte-Lovejoy. "Structure and Function of Protein Arginine Methyltransferase PRMT7." Life 11, no. 8 (2021): 768. http://dx.doi.org/10.3390/life11080768.

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PRMT7 is a member of the protein arginine methyltransferase (PRMT) family, which methylates a diverse set of substrates. Arginine methylation as a posttranslational modification regulates protein–protein and protein–nucleic acid interactions, and as such, has been implicated in various biological functions. PRMT7 is a unique, evolutionarily conserved PRMT family member that catalyzes the mono-methylation of arginine. The structural features, functional aspects, and compounds that inhibit PRMT7 are discussed here. Several studies have identified physiological substrates of PRMT7 and investigate

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33

SWIERCZ, Rafal, Maria D. PERSON, and Mark T. BEDFORD. "Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)." Biochemical Journal 386, no. 1 (2005): 85–91. http://dx.doi.org/10.1042/bj20041466.

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PRMT3 (protein arginine methyltransferase 3) is one of four type I arginine methyltransferases that catalyse the formation of asymmetric dimethylarginine. PRMT3 is unique in that its N-terminus harbours a C2H2 zinc-finger domain that is proposed to confer substrate specificity. In addition, PRMT3 is the only type I enzyme that is restricted to the cytoplasm. Known in vitro substrates for PRMT3 include GST–GAR (a glutathione S-transferase fusion protein containing the glycine- and arginine-rich N-terminal region of fibrillarin), Sam68 (Src-associated substrate during mitosis 68 kDa) and PABP-N1

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Lee, Yu-Jen, Wan-Yu Hsieh, Ling-Yun Chen, and Chuan Li. "Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution." Journal of Cellular Biochemistry 113, no. 8 (2012): 2721–28. http://dx.doi.org/10.1002/jcb.24151.

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Shailesh, Harshita, Zain Z. Zakaria, Robert Baiocchi, and Saïd Sif. "Protein arginine methyltransferase 5 (PRMT5) dysregulation in cancer." Oncotarget 9, no. 94 (2018): 36705–18. http://dx.doi.org/10.18632/oncotarget.26404.

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36

Palte, Rachel L., Sebastian E. Schneider, Michael D. Altman, et al. "Allosteric Modulation of Protein Arginine Methyltransferase 5 (PRMT5)." ACS Medicinal Chemistry Letters 11, no. 9 (2020): 1688–93. http://dx.doi.org/10.1021/acsmedchemlett.9b00525.

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37

Siarheyeva, Alena, Guillermo Senisterra, Abdellah Allali-Hassani, et al. "An Allosteric Inhibitor of Protein Arginine Methyltransferase 3." Structure 20, no. 8 (2012): 1425–35. http://dx.doi.org/10.1016/j.str.2012.06.001.

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38

Boivin, D., W. Lin, and R. Béliveau. "Essential arginine residues in isoprenylcysteine protein carboxyl methyltransferase." Biochemistry and Cell Biology 75, no. 1 (1997): 63–69. http://dx.doi.org/10.1139/o97-005.

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39

Obianyo, Obiamaka, and Paul R. Thompson. "Kinetic Mechanism of Protein Arginine Methyltransferase 6 (PRMT6)." Journal of Biological Chemistry 287, no. 8 (2012): 6062–71. http://dx.doi.org/10.1074/jbc.m111.333609.

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40

Sengupta, Shouvonik, Austin Kennemer, Kristin Patrick, Philip Tsichlis, and Mireia Guerau-de-Arellano. "Protein Arginine Methyltransferase 5 in T Lymphocyte Biology." Trends in Immunology 41, no. 10 (2020): 918–31. http://dx.doi.org/10.1016/j.it.2020.08.007.

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41

Guccione, Ernesto, Megan Schwarz, Federico Di Tullio, and Slim Mzoughi. "Cancer synthetic vulnerabilities to protein arginine methyltransferase inhibitors." Current Opinion in Pharmacology 59 (August 2021): 33–42. http://dx.doi.org/10.1016/j.coph.2021.04.004.

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42

Lafleur, Véronique N., Stéphane Richard, and Darren E. Richard. "Transcriptional repression of hypoxia-inducible factor-1 (HIF-1) by the protein arginine methyltransferase PRMT1." Molecular Biology of the Cell 25, no. 6 (2014): 925–35. http://dx.doi.org/10.1091/mbc.e13-07-0423.

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Hypoxia-inducible factors (HIF-1 and HIF-2) are essential mediators for the adaptive transcriptional response of cells and tissues to low-oxygen conditions. Under hypoxia or when cells are treated with various nonhypoxic stimuli, the active HIF-α subunits are mainly regulated through increased protein stabilization. For HIF-1α, it is clear that further transcriptional, translational, and posttranslational regulations are important for complete HIF-1 activity. Novel evidence links hypoxia and HIF-1 to arginine methylation, an important protein modification. These studies suggest that arginine m

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Shen, Yudao, Magdalena M. Szewczyk, Mohammad S. Eram, et al. "Discovery of a Potent, Selective, and Cell-Active Dual Inhibitor of Protein Arginine Methyltransferase 4 and Protein Arginine Methyltransferase 6." Journal of Medicinal Chemistry 59, no. 19 (2016): 9124–39. http://dx.doi.org/10.1021/acs.jmedchem.6b01033.

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44

Lee, Wei-Chao, Wen-Ling Lin, Tsutomu Matsui, et al. "Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity." Biochemistry 54, no. 51 (2015): 7514–23. http://dx.doi.org/10.1021/acs.biochem.5b00995.

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Yi, Meiqi, Yingying Ma, Yuling Chen, Chongdong Liu, Qingtao Wang, and Haiteng Deng. "Glutathionylation Decreases Methyltransferase Activity of PRMT5 and Inhibits Cell Proliferation." Molecular & Cellular Proteomics 19, no. 11 (2020): 1910–20. http://dx.doi.org/10.1074/mcp.ra120.002132.

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Glutathionylation is an important posttranslational modification that protects proteins from further oxidative damage as well as influencing protein structure and activity. In the present study, we demonstrate that the cysteine-42 residue in protein arginine N-methyltransferase 5 (PRMT5) is glutathionylated in aged mice or in cells that have been exposed to oxidative stress. Deglutathionylation of this protein is catalyzed by glutaredoxin-1 (Grx1). Using mutagenesis and subsequent biochemical analyses, we show that glutathionylation decreased the binding affinity of PRMT5 with methylosome prot

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Yan, Zhenzhen, Haifeng Wu, Hansen Liu, et al. "The protein arginine methyltransferase PRMT1 promotes TBK1 activation through asymmetric arginine methylation." Cell Reports 36, no. 12 (2021): 109731. http://dx.doi.org/10.1016/j.celrep.2021.109731.

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Pawlak, Maciej R., Christina A. Scherer, Jin Chen, Michael J. Roshon, and H. Earl Ruley. "Arginine N-Methyltransferase 1 Is Required for Early Postimplantation Mouse Development, but Cells Deficient in the Enzyme Are Viable." Molecular and Cellular Biology 20, no. 13 (2000): 4859–69. http://dx.doi.org/10.1128/mcb.20.13.4859-4869.2000.

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ABSTRACT Protein arginine N-methyltransferases have been implicated in a variety of processes, including cell proliferation, signal transduction, and protein trafficking. In this study, we have characterized essentially a null mutation induced by insertion of the U3βGeo gene trap retrovirus into the second intron of the mouse protein arginineN-methyltransferase 1 gene (Prmt1). cDNAs encoding two forms of Prmt1 were characterized, and the predicted protein sequences were found to be highly conserved among vertebrates. Expression of the Prmt1-βgeo fusion gene was greatest along the midline of th

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vanLieshout, Tiffany L., Jacob T. Bonafiglia, Brendon J. Gurd, and Vladimir Ljubicic. "Protein arginine methyltransferase biology in humans during acute and chronic skeletal muscle plasticity." Journal of Applied Physiology 127, no. 3 (2019): 867–80. http://dx.doi.org/10.1152/japplphysiol.00142.2019.

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Protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the methylation of arginine residues on target proteins. While dysregulation of PRMTs has been documented in a number of the most prevalent diseases, our understanding of PRMT biology in human skeletal muscle is limited. This study served to address this knowledge gap by exploring PRMT expression and function in human skeletal muscle in vivo and characterizing PRMT biology in response to acute and chronic stimuli for muscle plasticity. Fourteen untrained, healthy men performed one session of sprint interval exerc

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Rho, Jaerang, Seeyoung Choi, Young Rim Seong, Joonho Choi, and Dong-Soo Im. "The Arginine-1493 Residue in QRRGRTGR1493G Motif IV of the Hepatitis C Virus NS3 Helicase Domain Is Essential for NS3 Protein Methylation by the Protein Arginine Methyltransferase 1." Journal of Virology 75, no. 17 (2001): 8031–44. http://dx.doi.org/10.1128/jvi.75.17.8031-8044.2001.

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ABSTRACT The NS3 protein of hepatitis C virus (HCV) contains protease and RNA helicase activities, both of which are likely to be essential for HCV propagation. An arginine residue present in the arginine-glycine (RG)-rich region of many RNA-binding proteins is posttranslationally methylated by protein arginine methyltransferases (PRMTs). Amino acid sequence analysis revealed that the NS3 protein contains seven RG motifs, including two potential RG motifs in the 1486-QRRGRTGRG-1494 motif IV of the RNA helicase domain, in which arginines are potentially methylated by PRMTs. Indeed, we found tha

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Miranda, Tina Branscombe, Kristofor J. Webb, Dale D. Edberg, Raymond Reeves, and Steven Clarke. "Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a." Biochemical and Biophysical Research Communications 336, no. 3 (2005): 831–35. http://dx.doi.org/10.1016/j.bbrc.2005.08.179.

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