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Hui Liu, Xu Ma, Hua Nan Han, Yu Jin Hao, Xian Sheng Zhang
Protein arginine methylation plays essential roles in diverse biological processes, but its role in regulating shoot regeneration remains elusive. In this study, we analyzed the function of the protein arginine methyltransferase AtPRMT5 during de novo shoot regeneration in Arabidopsis. AtPRMT5 encodes a type II PRMT that methylates proteins, including histones and RNA splicing factors. Mutation of AtPMRT5 decreased the frequency of shoot regeneration and number of shoots per callus in the atprmt5 mutant compared with those of the wild type...
October 22, 2016: Molecular Plant
Anna Czarnecka, Krzysztof Milewski, Radosław Jaźwiec, Magdalena Zielińska
Alterations in brain nitric oxide (NO)/cGMP synthesis contribute to the pathogenesis of hepatic encephalopathy (HE). An increased asymmetrically dimethylated derivative of L-arginine (ADMA), an endogenous inhibitor of NO synthases, was observed in plasma of HE patients and animal models. It is not clear whether changes in brain ADMA reflect its increased local synthesis therefore affecting NO/cGMP pathway, or are a consequence of its increased peripheral blood content. We measured extracellular concentration of ADMA and symmetrically dimethylated isoform (SDMA) in the prefrontal cortex of control and thioacetamide (TAA)-induced HE rats...
September 8, 2016: Neurotoxicity Research
Wei-Chih Tsai, Sitaram Gayatri, Lucas C Reineke, Gianluca Sbardella, Mark T Bedford, Richard E Lloyd
Stress granules (SGs) are cytoplasmic condensates of stalled messenger ribonucleoprotein complexes (mRNPs) that form when eukaryotic cells encounter environmental stress. RNA binding proteins are enriched for arginine methylation and facilitate SG assembly through interactions involving regions of low amino acid complexity. How methylation of specific RNA binding proteins regulates RNA granule assembly has not been characterized. Here, we examined the potent SG nucleating protein Ras-GAP SH3 Binding Protein 1 (G3BP1), and found that G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain...
September 6, 2016: Journal of Biological Chemistry
Sara C Larsen, Kathrine B Sylvestersen, Andreas Mund, David Lyon, Meeli Mullari, Maria V Madsen, Jeremy A Daniel, Lars J Jensen, Michael L Nielsen
The posttranslational modification of proteins by arginine methylation is functionally important, yet the breadth of this modification is not well characterized. Using high-resolution mass spectrometry, we identified 8030 arginine methylation sites within 3300 human proteins in human embryonic kidney 293 cells, indicating that the occurrence of this modification is comparable to phosphorylation and ubiquitylation. A site-level conservation analysis revealed that arginine methylation sites are less evolutionarily conserved compared to arginines that were not identified as modified by methylation...
2016: Science Signaling
Coralie Poulard, Laura Corbo, Muriel Le Romancer
Protein arginine methylation is a common post-translational modification involved in numerous cellular processes including transcription, DNA repair, mRNA splicing and signal transduction. Currently, there are nine known members of the protein arginine methyltransferase (PRMT) family, but only one arginine demethylase has been identified, namely the Jumonji domain-containing 6 (JMJD6). Although its demethylase activity was initially challenged, its dual activity as an arginine demethylase and a lysine hydroxylase is now recognized...
August 18, 2016: Oncotarget
Symon Gathiaka, Brittany Boykin, Tamar Cáceres, Joan M Hevel, Orlando Acevedo
Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of specific arginyl groups within targeted proteins to regulate fundamental biological responses in eukaryotic cells. The major Type I PRMT enzyme, PRMT1, strictly generates monomethyl arginine (MMA) and asymmetric dimethylarginine (ADMA), but not symmetric dimethylarginine (SDMA). Multiple diseases can arise from the dysregulation of PRMT1, including heart disease and cancer, which underscores the need to elucidate the origin of product specificity...
October 15, 2016: Bioorganic & Medicinal Chemistry
Astrid Knuhtsen, Baptiste Legrand, Olivier Van der Poorten, Muriel Amblard, Jean Martinez, Steven Ballet, Jesper L Kristensen, Daniel Sejer Pedersen
Protein arginine N-methyl transferases (PRMTs) belong to a family of enzymes that modulate the epigenetic code through modifications of histones. In the present study, peptides emerging from a phage display screening were modified in the search for PRMT inhibitors through substitution with non-proteinogenic amino acids, N-alkylation of the peptide backbone, and incorporation of constrained dipeptide mimics. One of the modified peptides (23) showed an increased inhibitory activity towards several PRMTs in the low μm range and the conformational preference of this peptide was investigated and compared with the original hit using circular dichroism and NMR spectroscopy...
September 19, 2016: Chemistry: a European Journal
Emre Mutlu, Selçuk İlhan, Elif Onat, Murat Kara, Engin Şahna
BACKGROUND/AIM: The effects of AT2 receptor agonist novokinin on blood pressure, eNOS, NADPH oxidase, protein arginine methyltransferases (PRMTs), and Rho kinase in hypertension were investigated. Furthermore, in isolated thoracic aorta rings, contractile and dilator responses were studied. MATERIALS AND METHODS: To develop hypertension, L-NAME was administered intraperitoneally and salt was given with tap water (1%) for 4 weeks. Novokinin was administered intraperitoneally for the last 2 weeks...
2016: Turkish Journal of Medical Sciences
Thomas Schneider, Dietmar Ikemeyer, Sónia Ferreira, Ole Müller
Coenagrion persicum was described by Heinrich Lohmann in 1993 on the basis of a single male and two larvae captured in 1937 by E.W. Kaiser in Lorestãn Province (W-Iran). In June 2015 two of the authors (TS and DI) rediscovered individual-rich populations of this species in two Iranian provinces (Lorestãn and Esfahãn). We could confirm the structural differences of the male appendages between C. persicum and C. pulchellum based on a larger number of specimens than in the original description. The structural differences from C...
2016: Zootaxa
Renato Ferreira de Freitas, Mohammad S Eram, David Smil, Magdalena M Szewczyk, Steven Kennedy, Peter J Brown, Vijayaratnam Santhakumar, Dalia Barsyte-Lovejoy, Cheryl H Arrowsmith, Masoud Vedadi, Matthieu Schapira
Protein arginine methyltransferases (PRMTs) represent an emerging target class in oncology and other disease areas. So far, the most successful strategy to identify PRMT inhibitors has been to screen large to medium-size chemical libraries. Attempts to develop PRMT inhibitors using receptor-based computational methods have met limited success. Here, using virtual screening approaches, we identify 11 CARM1 (PRMT4) inhibitors with ligand efficiencies ranging from 0.28 to 0.84. CARM1 selective hits were further validated by orthogonal methods...
July 28, 2016: Journal of Medicinal Chemistry
Kanishk Jain, Rebeccah A Warmack, Erik W Debler, Andrea Hadjikyriacou, Peter Stavropoulos, Steven G Clarke
In the family of protein arginine methyltransferases (PRMTs) that predominantly generate either asymmetric or symmetric dimethylarginine (SDMA), PRMT7 is unique in producing solely monomethylarginine (MMA) products. The type of methylation on histones and other proteins dictates changes in gene expression, and numerous studies have linked altered profiles of methyl marks with disease phenotypes. Given the importance of specific inhibitor development, it is crucial to understand the mechanisms by which PRMT product specificity is conferred...
August 26, 2016: Journal of Biological Chemistry
Laura G Di Pasqua, Clarissa Berardo, Vittoria Rizzo, Plinio Richelmi, Anna Cleta Croce, Mariapia Vairetti, Andrea Ferrigno
Using an experimental model of NASH induced by a methionine-choline-deficient (MCD) diet, we investigated whether changes occur in serum and tissue levels of asymmetric dimethylarginine (ADMA). Male Wistar rats underwent NASH induced by 8-week feeding with an MCD diet. Serum and hepatic biopsies at 2, 4 and 8 weeks were taken, and serum enzymes, ADMA and nitrate/nitrite (NOx), were evaluated. Hepatic biopsies were used for mRNA and protein expression analysis of dimethylarginine dimethylaminohydrolase-1 (DDAH-1) and protein methyltransferases (PRMT-1), enzymes involved in ADMA metabolism and synthesis, respectively, and ADMA transporters (CAT-1, CAT-2A and CAT-2B)...
August 2016: Molecular and Cellular Biochemistry
Sitaram Gayatri, Martis W Cowles, Vidyasiri Vemulapalli, Donghang Cheng, Zu-Wen Sun, Mark T Bedford
Signal transduction in response to stimuli relies on the generation of cascades of posttranslational modifications that promote protein-protein interactions and facilitate the assembly of distinct signaling complexes. Arginine methylation is one such modification, which is catalyzed by a family of nine protein arginine methyltransferases, or PRMTs. Elucidating the substrate specificity of each PRMT will promote a better understanding of which signaling networks these enzymes contribute to. Although many PRMT substrates have been identified, and their methylation sites mapped, the optimal target motif for each of the nine PRMTs has not been systematically addressed...
2016: Scientific Reports
Yu Cao, Yuan Fang, Jianjun Mu, Xiaohong Liu
Endothelial dysfunction has an important role in the development and progression of salt-sensitive hypertension. Asymmetric dimethylarginine (ADMA), which is an endogenous inhibitor of nitric oxide synthase (NOS), has been demonstrated to be involved in the pathophysiological processes of endothelial dysfunction and salt‑sensitive hypertension. However, it is currently unclear how high salt intake may induce these processes. The present study investigated the effects of high salt medium on ADMA, endothelial NOS (eNOS) and the Ras homolog gene family, member A (RhoA)/Rho-associated protein kinase (ROCK) pathway in the EA...
July 2016: Molecular Medicine Reports
Lei Li, Zhengwen Zhang, Tengxiao Ma, Ran Huo
Overexpression of protein arginine methyltransferases (PRMTs) is associated with various types of cancer. The present study aimed to determine the expression level of PRMT1 in human melanoma and investigate its biological function. The clinical significance of PRMT1 was determined by screening the Oncomine database, and the increased expression of PRMT in melanoma was confirmed by western blot analysis. Furthermore, the current study demonstrated that PRMT1 was overexpressed in melanoma cell lines compared with human immortalized keratinocytes and PIG1 immortalized human melanocytes...
July 2016: Molecular Medicine Reports
Ji Hye Kim, Byong Chul Yoo, Woo Seok Yang, Eunji Kim, Sungyoul Hong, Jae Youl Cho
Protein arginine methyltransferases (PRMTs) mediate the methylation of a number of protein substrates of arginine residues and serve critical functions in many cellular responses, including cancer development, progression, and aggressiveness, T-lymphocyte activation, and hepatic gluconeogenesis. There are nine members of the PRMT family, which are divided into 4 types (types I-IV). Although most PRMTs do not require posttranslational modification (PTM) to be activated, fine-tuning modifications, such as interactions between cofactor proteins, subcellular compartmentalization, and regulation of RNA, via micro-RNAs, seem to be required...
2016: Mediators of Inflammation
Claudia Solari, Camila Vázquez Echegaray, Carlos Luzzani, María Soledad Cosentino, Ariel Waisman, María Victoria Petrone, Marcos Francia, Alina Sassone, Jésica Canizo, Gustavo Sevlever, Lino Barañao, Santiago Miriuka, Alejandra Guberman
Addition of methyl groups to arginine residues is catalyzed by a group of enzymes called Protein Arginine Methyltransferases (Prmt). Although Prmt1 is essential in development, its paralogue Prmt8 has been poorly studied. This gene was reported to be expressed in nervous system and involved in neurogenesis. In this work, we found that Prmt8 is expressed in mouse embryonic stem cells (ESC) and in induced pluripotent stem cells, and modulated along differentiation to neural precursor cells. We found that Prmt8 promoter activity is induced by the pluripotency transcription factors Oct4, Sox2 and Nanog...
April 22, 2016: Biochemical and Biophysical Research Communications
Sachiko Toma-Fukai, Jun-Dal Kim, Kyung-Eui Park, Naoyuki Kuwabara, Nobutaka Shimizu, Elena Krayukhina, Susumu Uchiyama, Akiyoshi Fukamizu, Toshiyuki Shimizu
Protein arginine methyltransferase 8 (PRMT8) is unique among PRMTs, as it is specifically expressed in brain and localized to the plasma membrane via N-terminal myristoylation. Here, we describe the crystal structure of human PRMT8 (hPRMT8) at 3.0-Å resolution. The crystal structure of hPRMT8 exhibited a novel helical assembly. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. This octameric structure is necessary for proper localization to the plasma membrane and efficient methyltransferase activity...
March 27, 2016: Journal of Molecular Biology
Erik W Debler, Kanishk Jain, Rebeccah A Warmack, You Feng, Steven G Clarke, Günter Blobel, Pete Stavropoulos
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...
February 23, 2016: Proceedings of the National Academy of Sciences of the United States of America
Kamal El Bissati, Elena S Suvorova, Hui Xiao, Olivier Lucas, Rajendra Upadhya, Yanfen Ma, Ruth Hogue Angeletti, Michael W White, Louis M Weiss, Kami Kim
UNLABELLED: The arginine methyltransferase family (PRMT) has been implicated in a variety of cellular processes, including signal transduction, epigenetic regulation, and DNA repair pathways. PRMT1 is thought to be responsible for the majority of PRMT activity in Toxoplasma gondii, but its exact function is unknown. To further define the biological function of the PRMT family, we generated T. gondii mutants lacking PRMT1 (Δprmt1) by deletion of the PRMT1 gene. Δprmt1 parasites exhibit morphological defects during cell division and grow slowly, and this phenotype reverses in the Δprmt::PRMT1mRFP complemented strain...
2016: MBio
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