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Artículos de revistas sobre el tema "Methyltransferase"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 26 de julio de 2025

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1

Wnuk, Maciej, Piotr Slipek, Mateusz Dziedzic, and Anna Lewinska. "The Roles of Host 5-Methylcytosine RNA Methyltransferases during Viral Infections." International Journal of Molecular Sciences 21, no. 21 (2020): 8176. http://dx.doi.org/10.3390/ijms21218176.

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Eukaryotic 5-methylcytosine RNA methyltransferases catalyze the transfer of a methyl group to the fifth carbon of a cytosine base in RNA sequences to produce 5-methylcytosine (m5C). m5C RNA methyltransferases play a crucial role in the maintenance of functionality and stability of RNA. Viruses have developed a number of strategies to suppress host innate immunity and ensure efficient transcription and translation for the replication of new virions. One such viral strategy is to use host m5C RNA methyltransferases to modify viral RNA and thus to affect antiviral host responses. Here, we summari

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2

Jeevarajah, Dharshini, John H. Patterson, Ellen Taig, Tobias Sargeant, Malcolm J. McConville, and Helen Billman-Jacobe. "Methylation of GPLs in Mycobacterium smegmatis and Mycobacterium avium." Journal of Bacteriology 186, no. 20 (2004): 6792–99. http://dx.doi.org/10.1128/jb.186.20.6792-6799.2004.

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ABSTRACT Several species of mycobacteria express abundant glycopeptidolipids (GPLs) on the surfaces of their cells. The GPLs are glycolipids that contain modified sugars including acetylated 6-deoxy-talose and methylated rhamnose. Four methyltransferases have been implicated in the synthesis of the GPLs of Mycobacterium smegmatis and Mycobacterium avium. A rhamnosyl 3-O-methytransferase and a fatty acid methyltransferase of M. smegmatis have been previously characterized. In this paper, we characterize the methyltransferases that are responsible for modifying the hydroxyl groups at positions 2

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3

Paul, Ligi, Donald J. Ferguson, and Joseph A. Krzycki. "The Trimethylamine Methyltransferase Gene and Multiple Dimethylamine Methyltransferase Genes of Methanosarcina barkeri Contain In-Frame and Read-Through Amber Codons." Journal of Bacteriology 182, no. 9 (2000): 2520–29. http://dx.doi.org/10.1128/jb.182.9.2520-2529.2000.

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ABSTRACT Three different methyltransferases initiate methanogenesis from trimethylamine (TMA), dimethylamine (DMA) or monomethylamine (MMA) by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M (CoM). Here, genes encoding the DMA and TMA methyltransferases are characterized for the first time. A single copy of mttB, the TMA methyltransferase gene, was cotranscribed with a copy of the DMA methyltransferase gene,mtbB1. However, two other nearly identical copies ofmtbB1, designated mtbB2 and mtbB3, were also found in the genome. A 6.8-kb transcript

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4

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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5

Savic, Miloje, S. Sunita, Natalia Zelinskaya, et al. "30S Subunit-Dependent Activation of the Sorangium cellulosum So ce56 Aminoglycoside Resistance-Conferring 16S rRNA Methyltransferase Kmr." Antimicrobial Agents and Chemotherapy 59, no. 5 (2015): 2807–16. http://dx.doi.org/10.1128/aac.00056-15.

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ABSTRACTMethylation of bacterial 16S rRNA within the ribosomal decoding center confers exceptionally high resistance to aminoglycoside antibiotics. This resistance mechanism is exploited by aminoglycoside producers for self-protection while functionally equivalent methyltransferases have been acquired by human and animal pathogenic bacteria. Here, we report structural and functional analyses of theSorangium cellulosumSo ce56 aminoglycoside resistance-conferring methyltransferase Kmr. Our results demonstrate that Kmr is a 16S rRNA methyltransferase acting at residue A1408 to confer a canonical

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6

Zhang, Jianyu, and Judith P. Klinman. "Convergent Mechanistic Features between the Structurally DiverseN- andO-Methyltransferases: GlycineN-Methyltransferase and CatecholO-Methyltransferase." Journal of the American Chemical Society 138, no. 29 (2016): 9158–65. http://dx.doi.org/10.1021/jacs.6b03462.

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7

Corrêa, Laís L., Marta A. Witek, Natalia Zelinskaya, Renata C. Picão, and Graeme L. Conn. "Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG." Antimicrobial Agents and Chemotherapy 60, no. 1 (2015): 699–702. http://dx.doi.org/10.1128/aac.02482-15.

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ABSTRACTThe exogenously acquired 16S rRNA methyltransferases RmtD, RmtD2, and RmtG were cloned and heterologously expressed inEscherichia coli, and the recombinant proteins were purified to near homogeneity. Each methyltransferase conferred an aminoglycoside resistance profile consistent with m7G1405 modification, and this activity was confirmed byinvitro30S methylation assays. Analyses of protein structure and interaction withS-adenosyl-l-methionine suggest that the molecular mechanisms of substrate recognition and catalysis are conserved across the 16S rRNA (m7G1405) methyltransferase family

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8

Nyyssölä, Antti, Tapani Reinikainen, and Matti Leisola. "Characterization of Glycine SarcosineN-Methyltransferase and Sarcosine DimethylglycineN-Methyltransferase." Applied and Environmental Microbiology 67, no. 5 (2001): 2044–50. http://dx.doi.org/10.1128/aem.67.5.2044-2050.2001.

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ABSTRACT Glycine betaine is accumulated in cells living in high salt concentrations to balance the osmotic pressure. Glycine sarcosineN-methyltransferase (GSMT) and sarcosine dimethylglycineN-methyltransferase (SDMT) of Ectothiorhodospira halochloris catalyze the threefold methylation of glycine to betaine, with S-adenosylmethionine acting as the methyl group donor. These methyltransferases were expressed inEscherichia coli and purified, and some of their enzymatic properties were characterized. Both enzymes had high substrate specificities and pH optima near the physiological pH. No evidence

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9

Ruszkowska, Agnieszka. "METTL16, Methyltransferase-Like Protein 16: Current Insights into Structure and Function." International Journal of Molecular Sciences 22, no. 4 (2021): 2176. http://dx.doi.org/10.3390/ijms22042176.

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Methyltransferase-like protein 16 (METTL16) is a human RNA methyltransferase that installs m6A marks on U6 small nuclear RNA (U6 snRNA) and S-adenosylmethionine (SAM) synthetase pre-mRNA. METTL16 also controls a significant portion of m6A epitranscriptome by regulating SAM homeostasis. Multiple molecular structures of the N-terminal methyltransferase domain of METTL16, including apo forms and complexes with S-adenosylhomocysteine (SAH) or RNA, provided the structural basis of METTL16 interaction with the coenzyme and substrates, as well as indicated autoinhibitory mechanism of the enzyme activ

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10

Mashhoon, Neda, Cynthia Pruss, Michael Carroll, Paul H. Johnson, and Norbert O. Reich. "Selective Inhibitors of Bacterial DNA Adenine Methyltransferases." Journal of Biomolecular Screening 11, no. 5 (2006): 497–510. http://dx.doi.org/10.1177/1087057106287933.

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The authors describe the discovery and characterization of several structural classes of small-molecule inhibitors of bacterial DNA adenine methyltransferases. These enzymes are essential for bacterial virulence (DNA adenine methyltransferase [DAM]) and cell viability (cell cycle–regulated methyltransferase [CcrM]). Using a novel high-throughput fluorescence-based assay and recombinant DAM and CcrM, the authors screened a diverse chemical library. They identified 5 major structural classes of inhibitors composed of more than 350 compounds: cyclopentaquinolines, phenyl vinyl furans, pyrimidine-

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11

Goll, Mary Grace, Finn Kirpekar, Keith A. Maggert, et al. "Methylation of tRNAAsp by the DNA Methyltransferase Homolog Dnmt2." Science 311, no. 5759 (2006): 395–98. http://dx.doi.org/10.1126/science.1120976.

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The sequence and the structure of DNA methyltransferase-2 (Dnmt2) bear close affinities to authentic DNA cytosine methyltransferases. A combined genetic and biochemical approach revealed that human DNMT2 did not methylate DNA but instead methylated a small RNA; mass spectrometry showed that this RNA is aspartic acid transfer RNA (tRNAAsp) and that DNMT2 specifically methylated cytosine 38 in the anticodon loop. The function of DNMT2 is highly conserved, and human DNMT2 protein restored methylation in vitro to tRNAAsp from Dnmt2-deficient strains of mouse, Arabidopsis thaliana, and Drosophila m

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12

Tomikawa, Chie. "7-Methylguanosine Modifications in Transfer RNA (tRNA)." International Journal of Molecular Sciences 19, no. 12 (2018): 4080. http://dx.doi.org/10.3390/ijms19124080.

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More than 90 different modified nucleosides have been identified in tRNA. Among the tRNA modifications, the 7-methylguanosine (m7G) modification is found widely in eubacteria, eukaryotes, and a few archaea. In most cases, the m7G modification occurs at position 46 in the variable region and is a product of tRNA (m7G46) methyltransferase. The m7G46 modification forms a tertiary base pair with C13-G22, and stabilizes the tRNA structure. A reaction mechanism for eubacterial tRNA m7G methyltransferase has been proposed based on the results of biochemical, bioinformatic, and structural studies. How

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13

Scharnagl, Matthias, Stefan Richter, and Martin Hagemann. "The Cyanobacterium Synechocystis sp. Strain PCC 6803 Expresses a DNA Methyltransferase Specific for the Recognition Sequence of the Restriction Endonuclease PvuI." Journal of Bacteriology 180, no. 16 (1998): 4116–22. http://dx.doi.org/10.1128/jb.180.16.4116-4122.1998.

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ABSTRACT By use of restriction endonucleases, the DNA of the cyanobacteriumSynechocystis sp. strain PCC 6803 was analyzed for DNA-specific methylation. Three different recognition sites of methyltransferases, a dam-like site including N6-methyladenosine and two other sites with methylcytosine, were identified, whereas no activities of restriction endonucleases could be detected in this strain. slr0214, aSynechocystis gene encoding a putative methyltransferase that shows significant similarities to C5-methylcytosine-synthesizing enzymes, was amplified by PCR and cloned for further characterizat

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14

Vale, Filipa F., and Jorge M. B. Vítor. "Genomic Methylation: a Tool for Typing Helicobacter pylori Isolates." Applied and Environmental Microbiology 73, no. 13 (2007): 4243–49. http://dx.doi.org/10.1128/aem.00199-07.

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ABSTRACT The genome sequences of three Helicobacter pylori strains revealed an abundant number of putative restriction and modification (R-M) systems within a small genome (1.60 to 1.67 Mb). Each R-M system includes an endonuclease that cleaves a specific DNA sequence and a DNA methyltransferase that methylates either adenosine or cytosine within the same DNA sequence. These are believed to be a defense mechanism, protecting bacteria from foreign DNA. They have been classified as selfish genetic elements; in some instances it has been shown that they are not easily lost from their host cell. P

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15

Filonov, V. L., M. A. Khomutov, A. V. Sergeev, et al. "Interaction of DNA Methyltransferase Dnmt3a with Phosphorus Analogs of S-Adenosylmethionine and S-Adenosylhomocysteine." Molecular Biology 57, no. 4 (2023): 747–54. http://dx.doi.org/10.1134/s0026893323040064.

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Abstract Enzymatic methyltransferase reactions are of crucial importance for cell metabolism. S-Adenosyl-L-methionine (AdoMet) is a main donor of the methyl group. DNA, RNA, proteins, and low-molecular-weight compounds are substrates of methyltransferases. In mammals, DNA methyltransferase Dnmt3a de novo methylates the C5 position of cytosine residues in CpG sequences in DNA. The methylation pattern is one of the factors that determine the epigenetic regulation of gene expression. Here, interactions with the catalytic domain of Dnmt3a was for the first time studied for phosphonous and phosphon

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16

Ramdhan, Peter, and Chenglong Li. "Targeting Viral Methyltransferases: An Approach to Antiviral Treatment for ssRNA Viruses." Viruses 14, no. 2 (2022): 379. http://dx.doi.org/10.3390/v14020379.

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Methyltransferase enzymes have been associated with different processes within cells and viruses. Specifically, within viruses, methyltransferases are used to form the 5′cap-0 structure for optimal evasion of the host innate immune system. In this paper, we seek to discuss the various methyltransferases that exist within single-stranded RNA (ssRNA) viruses along with their respective inhibitors. Additionally, the importance of motifs such as the KDKE tetrad and glycine-rich motif in the catalytic activity of methyltransferases is discussed.

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17

Falnes, Pål Ø., Magnus E. Jakobsson, Erna Davydova, Angela Ho та Jędrzej Małecki. "Protein lysine methylation by seven-β-strand methyltransferases". Biochemical Journal 473, № 14 (2016): 1995–2009. http://dx.doi.org/10.1042/bcj20160117.

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Lysine methylation is an important post-translational protein modification, and a number of novel lysine-specific protein methyltransferases belonging to the seven-β-strand methyltransferase family have recently been discovered. This article provides a comprehensive review of this group of enzymes.

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18

Jacques-Fricke, Bridget T., and Laura S. Gammill. "Neural crest specification and migration independently require NSD3-related lysine methyltransferase activity." Molecular Biology of the Cell 25, no. 25 (2014): 4174–86. http://dx.doi.org/10.1091/mbc.e13-12-0744.

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Neural crest precursors express genes that cause them to become migratory, multipotent cells, distinguishing them from adjacent stationary neural progenitors in the neurepithelium. Histone methylation spatiotemporally regulates neural crest gene expression; however, the protein methyltransferases active in neural crest precursors are unknown. Moreover, the regulation of methylation during the dynamic process of neural crest migration is unclear. Here we show that the lysine methyltransferase NSD3 is abundantly and specifically expressed in premigratory and migratory neural crest cells. NSD3 ex

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19

Fan, Yongfei, Xinwei Li, Huihui Sun, Zhaojia Gao, Zheng Zhu, and Kai Yuan. "Role of WTAP in Cancer: From Mechanisms to the Therapeutic Potential." Biomolecules 12, no. 9 (2022): 1224. http://dx.doi.org/10.3390/biom12091224.

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Wilms’ tumor 1-associating protein (WTAP) is required for N6-methyladenosine (m6A) RNA methylation modifications, which regulate biological processes such as RNA splicing, cell proliferation, cell cycle, and embryonic development. m6A is the predominant form of mRNA modification in eukaryotes. WTAP exerts m6A modification by binding to methyltransferase-like 3 (METTL3) in the nucleus to form the METTL3-methyltransferase-like 14 (METTL14)-WTAP (MMW) complex, a core component of the methyltransferase complex (MTC), and localizing to the nuclear patches. Studies have demonstrated that WTAP plays

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20

Brosnan, John T., Rene L. Jacobs, Lori M. Stead, and Margaret E. Brosnan. "Methylation demand: a key determinant of homocysteine metabolism." Acta Biochimica Polonica 51, no. 2 (2004): 405–13. http://dx.doi.org/10.18388/abp.2004_3580.

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Elevated plasma homocysteine is a risk factor for cardiovascular disease and Alzheimer's disease. To understand the factors that determine the plasma homocysteine level it is necessary to appreciate the processes that produce homocysteine and those that remove it. Homocysteine is produced as a result of methylation reactions. Of the many methyltransferases, two are, normally, of the greatest quantitative importance. These are guanidinoacetate methyltransferase (that produces creatine) and phosphatidylethanolamine N-methyltransferase (that produces phosphatidylcholine). In addition, methylation

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21

Ильинский, И. В., Е. М. Козлова, С. Х. Дегтярев, Н. К. Янковский та В. Ю. Макеев. "ЭФФЕКТИВНОСТЬ ОПРЕДЕЛЕНИЯ 5-МЕТИЛЦИТОЗИНА В ДНК КЛЕТОК ESCHERICHIA COLI, НЕСУЩИХ ГЕНЫ БАКТЕРИАЛЬНЫХ ДНК- МЕТИЛТРАНСФЕРАЗ, С ПОМОЩЬЮ УСТАНОВКИ OXFORD NANOPORE". Биофизика 65, № 6 (2020): 1045–50. http://dx.doi.org/10.31857/s0006302920060010.

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The MinION system (Oxford Nanopore Technologies Limited) was used for direct sequencing of genomic DNA of two recombinant E. coli strains. In one case, the cells contained a plasmid with the M.HpaII gene of DNA methyltransferase, which methylates the second cytosine in CCGG site; in the second case, the E. coli strain contained M.HspAI DNA methyltransferase, which modifies the central cytosine in the GCGC sequence. In both cases, DNA methyltransferases methylate cytosine to 5-methylcytosine. It has been shown that when DNA is sequenced at high coverage, the presence of 5-methylcytosine in DNA

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22

van Tran, Nhan, Felix G. M. Ernst, Ben R. Hawley, et al. "The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112." Nucleic Acids Research 47, no. 15 (2019): 7719–33. http://dx.doi.org/10.1093/nar/gkz619.

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Abstract N6-methyladenosine (m6A) has recently been found abundantly on messenger RNA and shown to regulate most steps of mRNA metabolism. Several important m6A methyltransferases have been described functionally and structurally, but the enzymes responsible for installing one m6A residue on each subunit of human ribosomes at functionally important sites have eluded identification for over 30 years. Here, we identify METTL5 as the enzyme responsible for 18S rRNA m6A modification and confirm ZCCHC4 as the 28S rRNA modification enzyme. We show that METTL5 must form a heterodimeric complex with T

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23

Furuta, Yoshikazu, Fumihito Miura, Takahiro Ichise, et al. "A GCDGC-specific DNA (cytosine-5) methyltransferase that methylates the GCWGC sequence on both strands and the GCSGC sequence on one strand." PLOS ONE 17, no. 3 (2022): e0265225. http://dx.doi.org/10.1371/journal.pone.0265225.

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5-Methylcytosine is one of the major epigenetic marks of DNA in living organisms. Some bacterial species possess DNA methyltransferases that modify cytosines on both strands to produce fully-methylated sites or on either strand to produce hemi-methylated sites. In this study, we characterized a DNA methyltransferase that produces two sequences with different methylation patterns: one methylated on both strands and another on one strand. M.BatI is the orphan DNA methyltransferase of Bacillus anthracis coded in one of the prophages on the chromosome. Analysis of M.BatI modified DNA by bisulfite

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24

McGann, Patrick, Sarah Chahine, Darius Okafor, et al. "Detecting 16S rRNA Methyltransferases in Enterobacteriaceae by Use of Arbekacin." Journal of Clinical Microbiology 54, no. 1 (2015): 208–11. http://dx.doi.org/10.1128/jcm.02642-15.

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16S rRNA methyltransferases confer resistance to most aminoglycosides, but discriminating their activity from that of aminoglycoside-modifying enzymes (AMEs) is challenging using phenotypic methods. We demonstrate that arbekacin, an aminoglycoside refractory to most AMEs, can rapidly detect 16S methyltransferase activity inEnterobacteriaceaewith high specificity using the standard disk susceptibility test.

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Kostyushev, D. S., A. P. Zueva, S. A. Brezgin, et al. "Overexpression of DNA-methyltransferases in persistency of cccDNA pool in chronic hepatitis B." Terapevticheskii arkhiv 89, no. 11 (2017): 21–26. http://dx.doi.org/10.17116/terarkh2017891121-26.

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Aim. To define the role of DNA-methyltransferases of type 1 and type 3A in hepatitis B viral cycle. Materials and methods. Human hepatoma cells HepG2 with stable expression of 1.1-mer HBV genome were transfected with vectors encoding DNA-methyltransferase 1 (DNMT1), DNA-methyltransferase 3A (DNMT3A) or were co-transfected with these vectors. Total HBV DNA copy number, relative expression of pregenomic RNA (pgRNA), S-protein-encoding RNA (S-RNA) and cccDNA were analyzed by quantitative and semi-quantitative real-time PCR-analysis with TaqMan probes for assessment of DNMTs-mediated effects on HB

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Fukuda, Kei, and Yoichi Shinkai. "SETDB1-Mediated Silencing of Retroelements." Viruses 12, no. 6 (2020): 596. http://dx.doi.org/10.3390/v12060596.

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SETDB1 (SET domain bifurcated histone lysine methyltransferase 1) is a protein lysine methyltransferase and methylates histone H3 at lysine 9 (H3K9). Among other H3K9 methyltransferases, SETDB1 and SETDB1-mediated H3K9 trimethylation (H3K9me3) play pivotal roles for silencing of endogenous and exogenous retroelements, thus contributing to genome stability against retroelement transposition. Furthermore, SETDB1 is highly upregulated in various tumor cells. In this article, we describe recent advances about how SETDB1 activity is regulated, how SETDB1 represses various types of retroelements suc

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Meena, Laxman S., Puneet Chopra, Ram A. Vishwakarma, and Yogendra Singh. "Biochemical characterization of an S-adenosyl-l-methionine-dependent methyltransferase (Rv0469) of Mycobacterium tuberculosis." Biological Chemistry 394, no. 7 (2013): 871–77. http://dx.doi.org/10.1515/hsz-2013-0126.

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Abstract Tuberculostearic acid (l0-methylstearic acid, TSA) is a major constituent of mycobacterial membrane phospholipids, and its biosynthesis involves the direct methylation of oleic acid esterified as a component of phospholipids. The methyltransferases of mycobacteria were long proposed to be involved in the synthesis of methyl-branched short-chain fatty acids, but direct experimental evidence is still lacking. In this study, we identified the methyltransferase encoded by umaA in Mycobacterium tuberculosis H37Rv as a novel S-adenosyl-l-methionine (SAM)-dependent methyltransferase capable

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Weinshilboum, Richard M., Diane M. Otterness, and Carol L. Szumlanski. "METHYLATION PHARMACOGENETICS: Catechol O-Methyltransferase, Thiopurine Methyltransferase, and Histamine N-Methyltransferase." Annual Review of Pharmacology and Toxicology 39, no. 1 (1999): 19–52. http://dx.doi.org/10.1146/annurev.pharmtox.39.1.19.

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Jindal, Arshita, Anjali Sharma, and Neeraj Agarwal. "Quantitative Structure-Activity Relationship and Molecular Modeling Studies on a series of constrained (L-)-S-adenosyl-L-homocysteine (SAH) analogues acting as DNA methyltransferase inhibitors." Der Pharma Chemica 13, no. 1 (2021): 13. https://doi.org/10.5281/zenodo.13643569.

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DNA methyltransferases catalyses the transfer of methyl group to DNA. However, in the current study, a series of DNA methyltransferase inhibitors and new compound with better efficacy were predicted. Hence quantitative structure activity relationship (QSAR) studies were done on the series of constrained (L-)-S-adenosyl-L-homocysteine (SAH) analogues acting as DNA methyltransferase inhibitors, and afterwards followed by molecular modelling which gives cross-validated result (r 2 cv) of 0.653 carried out by Leave one out (LOO) method, and predicted (r 2 pred.) is 0.600 with coefficient of correl

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30

Husain, Nilofer, Karolina L. Tkaczuk, Rajesh T. Shenoy, et al. "Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m 7 G methyltransferases." Nucleic Acids Research 38, no. 12 (2010): 4120–32. http://dx.doi.org/10.1093/nar/gkq122.

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Abstract Sgm (Sisomicin-gentamicin methyltransferase) from antibiotic-producing bacterium Micromonospora zionensis is an enzyme that confers resistance to aminoglycosides like gentamicin and sisomicin by specifically methylating G1405 in bacterial 16S rRNA. Sgm belongs to the aminoglycoside resistance methyltransferase (Arm) family of enzymes that have been recently found to spread by horizontal gene transfer among disease-causing bacteria. Structural characterization of Arm enzymes is the key to understand their mechanism of action and to develop inhibitors that would block their activity. He

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31

Piechulla, Birgit, Nancy Magnus, Marie Chantal Lemfack, and Stephan Von Reuss. "Neue Klasse von Methyltransferasen mit Zyklisierungsaktivität." BIOspektrum 27, no. 1 (2021): 31–33. http://dx.doi.org/10.1007/s12268-021-1506-8.

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AbstractMicroorganisms release small volatile metabolites with unique structures, e. g. the polymethylated homosesquiterpene sodorifen from Serratia plymuthica. Two unusual enzymes with novel features are involved in its biosynthesis, a C-methyltransferase with cyclization activity and a terpene synthase that accepts a non-canonical monocyclic C16 substrate. The novel class of methyltransferases represents an alternative route that enlarges terpene diversity.

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Nosrati, Meisam, Debayan Dey, Atousa Mehrani, et al. "Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition." Journal of Biological Chemistry 294, no. 46 (2019): 17642–53. http://dx.doi.org/10.1074/jbc.ra119.011181.

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Methylation of the small ribosome subunit rRNA in the ribosomal decoding center results in exceptionally high-level aminoglycoside resistance in bacteria. Enzymes that methylate 16S rRNA on N7 of nucleotide G1405 (m7G1405) have been identified in both aminoglycoside-producing and clinically drug-resistant pathogenic bacteria. Using a fluorescence polarization 30S-binding assay and a new crystal structure of the methyltransferase RmtC at 3.14 Å resolution, here we report a structure-guided functional study of 30S substrate recognition by the aminoglycoside resistance-associated 16S rRNA (m7G140

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Hsieh, Chih-Lin. "In Vivo Activity of Murine De Novo Methyltransferases, Dnmt3a and Dnmt3b." Molecular and Cellular Biology 19, no. 12 (1999): 8211–18. http://dx.doi.org/10.1128/mcb.19.12.8211.

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ABSTRACT The putative de novo methyltransferases, Dnmt3a and Dnmt3b, were reported to have weak methyltransferase activity in methylating the 3′ long terminal repeat of Moloney murine leukemia virus in vitro. The activity of these enzymes was evaluated in vivo, using a stable episomal system that employs plasmids as targets for DNA methylation in human cells. De novo methylation of a subset of the CpG sites on the stable episomes is detected in human cells overexpressing the murine Dnmt3a or Dnmt3b1 protein. This de novo methylation activity is abolished when the cysteine in the P-C motif, whi

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Schilhabel, Anke, Sandra Studenik, Martin Vödisch, et al. "The Ether-Cleaving Methyltransferase System of the Strict Anaerobe Acetobacterium dehalogenans: Analysis and Expression of the Encoding Genes." Journal of Bacteriology 191, no. 2 (2008): 588–99. http://dx.doi.org/10.1128/jb.01104-08.

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ABSTRACT Anaerobic O-demethylases are inducible multicomponent enzymes which mediate the cleavage of the ether bond of phenyl methyl ethers and the transfer of the methyl group to tetrahydrofolate. The genes of all components (methyltransferases I and II, CP, and activating enzyme [AE]) of the vanillate- and veratrol-O-demethylases of Acetobacterium dehalogenans were sequenced and analyzed. In A. dehalogenans, the genes for methyltransferase I, CP, and methyltransferase II of both O-demethylases are clustered. The single-copy gene for AE is not included in the O-demethylase gene clusters. It w

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35

Ashihara, Hiroshi. "Biosynthetic Pathways of Purine and Pyridine Alkaloids in Coffee Plants." Natural Product Communications 11, no. 7 (2016): 1934578X1601100. http://dx.doi.org/10.1177/1934578x1601100742.

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Caffeine (1,3,7- N-trimethylxanthine) and trigonelline (1 N-methylnicotinic acid) are major alkaloids in coffee plants. The key enzymes involved in the biosynthesis of these compounds are very closely related N-methyltransferases belonging to the motif B’ family of methyltransferases. The major biosynthetic pathways of caffeine and trigonelline are summarized in this review, including new evidence obtained from recombinant enzymes. In addition, precursor supply pathways are discussed with newly obtained results. Transgenic plants produced by the modification of the expression of N-methyltransf

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Dong, Hongping, Katja Fink, Roland Züst, Siew Pheng Lim, Cheng-Feng Qin, and Pei-Yong Shi. "Flavivirus RNA methylation." Journal of General Virology 95, no. 4 (2014): 763–78. http://dx.doi.org/10.1099/vir.0.062208-0.

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The 5′ end of eukaryotic mRNA contains the type-1 (m7GpppNm) or type-2 (m7GpppNmNm) cap structure. Many viruses have evolved various mechanisms to develop their own capping enzymes (e.g. flavivirus and coronavirus) or to ‘steal’ caps from host mRNAs (e.g. influenza virus). Other viruses have developed ‘cap-mimicking’ mechanisms by attaching a peptide to the 5′ end of viral RNA (e.g. picornavirus and calicivirus) or by having a complex 5′ RNA structure (internal ribosome entry site) for translation initiation (e.g. picornavirus, pestivirus and hepacivirus). Here we review the diverse viral RNA

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37

Yan, Qiaoling, Neil Shaw, Lanfang Qian, and Dunquan Jiang. "Crystal structure of Rv1220c, a SAM-dependentO-methyltransferase fromMycobacterium tuberculosis." Acta Crystallographica Section F Structural Biology Communications 73, no. 6 (2017): 315–20. http://dx.doi.org/10.1107/s2053230x17006057.

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Rv1220c fromMycobacterium tuberculosisis annotated as anO-methyltransferase (MtbOMT). Currently, no structural information is available for this protein. Here, the crystal structure ofMtbOMT refined to 2.0 Å resolution is described. The structure reveals the presence of a methyltransferase fold and shows clear electron density for one molecule ofS-adenosylmethionine (SAM), which was apparently bound by the protein during its production inEscherichia coli. Although the overall structure ofMtbOMT resembles the structures ofO-methyltransferases fromCornybacterium glutamicum,Coxiella burnettiandAl

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38

White, Joshua, Zhihua Li, Richa Sardana, Janusz M. Bujnicki, Edward M. Marcotte, and Arlen W. Johnson. "Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits." Molecular and Cellular Biology 28, no. 10 (2008): 3151–61. http://dx.doi.org/10.1128/mcb.01674-07.

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ABSTRACT BUD23 was identified from a bioinformatics analysis of Saccharomyces cerevisiae genes involved in ribosome biogenesis. Deletion of BUD23 leads to severely impaired growth, reduced levels of the small (40S) ribosomal subunit, and a block in processing 20S rRNA to 18S rRNA, a late step in 40S maturation. Bud23 belongs to the S-adenosylmethionine-dependent Rossmann-fold methyltransferase superfamily and is related to small-molecule methyltransferases. Nevertheless, we considered that Bud23 methylates rRNA. Methylation of G1575 is the only mapped modification for which the methylase has n

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39

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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40

Dong, Hongping, Suping Ren, Bo Zhang, et al. "West Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning Mechanism." Journal of Virology 82, no. 9 (2008): 4295–307. http://dx.doi.org/10.1128/jvi.02202-07.

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ABSTRACT Flaviviruses encode a single methyltransferase domain that sequentially catalyzes two methylations of the viral RNA cap, GpppA-RNA→m7GpppA-RNA→m7GpppAm-RNA, by using S-adenosyl-l-methionine (SAM) as a methyl donor. Crystal structures of flavivirus methyltransferases exhibit distinct binding sites for SAM, GTP, and RNA molecules. Biochemical analysis of West Nile virus methyltransferase shows that the single SAM-binding site donates methyl groups to both N7 and 2′-O positions of the viral RNA cap, the GTP-binding pocket functions only during the 2′-O methylation, and two distinct sets

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41

Kim, Min Jung, Sung Un Huh, Byung-Kook Ham, and Kyung-Hee Paek. "A Novel Methyltransferase Methylates Cucumber Mosaic Virus 1a Protein and Promotes Systemic Spread." Journal of Virology 82, no. 10 (2008): 4823–33. http://dx.doi.org/10.1128/jvi.02518-07.

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ABSTRACT In mammalian and yeast systems, methyltransferases have been implicated in the regulation of diverse processes, such as protein-protein interactions, protein localization, signal transduction, RNA processing, and transcription. The Cucumber mosaic virus (CMV) 1a protein is essential not only for virus replication but also for movement. Using a yeast two-hybrid system with tobacco plants, we have identified a novel gene encoding a methyltransferase that interacts with the CMV 1a protein and have designated this gene Tcoi1 (tobacco CMV 1a-interacting protein 1). Tcoi1 specifically inter

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42

Lerouge, I., C. Verreth, J. Michiels, et al. "Three Genes Encoding for Putative Methyl- and Acetyltransferases Map Adjacent to the wzm and wzt Genes and Are Essential for O-Antigen Biosynthesis in Rhizobium etli CE3." Molecular Plant-Microbe Interactions® 16, no. 12 (2003): 1085–93. http://dx.doi.org/10.1094/mpmi.2003.16.12.1085.

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The elucidation of the structure of the O-antigen of Rhizo-bium etli CE3 predicts that the R. etli CE3 genome must contain genes encoding acetyl- and methyltransferases to confer the corresponding modifications to the O-antigen. We identified three open reading frames (ORFs) upstream of wzm, encoding the membrane component of the O-antigen transporter and located in the lpsα-region of R. etli CE3. The ORFs encode two putative acetyltransferases with similarity to the CysE-LacA-LpxA-NodL family of acetyl-transferases and one putative methyltransferase with sequence motifs common to a wide range

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43

Rowe, Sebastian J., Ryan J. Mecaskey, Mohamed Nasef, et al. "Shared requirements for key residues in the antibiotic resistance enzymes ErmC and ErmE suggest a common mode of RNA recognition." Journal of Biological Chemistry 295, no. 51 (2020): 17476–85. http://dx.doi.org/10.1074/jbc.ra120.014280.

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Erythromycin-resistance methyltransferases are SAM dependent Rossmann fold methyltransferases that convert A2058 of 23S rRNA to m62A2058. This modification sterically blocks binding of several classes of antibiotics to 23S rRNA, resulting in a multidrug-resistant phenotype in bacteria expressing the enzyme. ErmC is an erythromycin resistance methyltransferase found in many Gram-positive pathogens, whereas ErmE is found in the soil bacterium that biosynthesizes erythromycin. Whether ErmC and ErmE, which possess only 24% sequence identity, use similar structural elements for rRNA substrate recog

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Abeykoon, Amila H., Chien-Chung Chao, Guanghui Wang, Marjan Gucek, David C. H. Yang, and Wei-Mei Ching. "Two Protein Lysine Methyltransferases Methylate Outer Membrane Protein B from Rickettsia." Journal of Bacteriology 194, no. 23 (2012): 6410–18. http://dx.doi.org/10.1128/jb.01379-12.

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ABSTRACTRickettsia prowazekii, the etiologic agent of epidemic typhus, is a potential biological threat agent. Its outer membrane protein B (OmpB) is an immunodominant antigen and plays roles as protective envelope and as adhesins. The observation of the correlation between methylation of lysine residues in rickettsial OmpB and bacterial virulence has suggested the importance of an enzymatic system for the methylation of OmpB. However, no rickettsial lysine methyltransferase has been characterized. Bioinformatic analysis of genomic DNA sequences ofRickettsiaidentified putative lysine methyltra

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45

Mathur, Yamini, Sheryl Sreyas, Prathamesh M. Datar, Manjima B. Sathian, and Amrita B. Hazra. "CobT and BzaC catalyze the regiospecific activation and methylation of the 5-hydroxybenzimidazole lower ligand in anaerobic cobamide biosynthesis." Journal of Biological Chemistry 295, no. 31 (2020): 10522–34. http://dx.doi.org/10.1074/jbc.ra120.014197.

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Vitamin B12 and other cobamides are essential cofactors required by many organisms and are synthesized by a subset of prokaryotes via distinct aerobic and anaerobic routes. The anaerobic biosynthesis of 5,6-dimethylbenzimidazole (DMB), the lower ligand of vitamin B12, involves five reactions catalyzed by the bza operon gene products, namely the hydroxybenzimidazole synthase BzaAB/BzaF, phosphoribosyltransferase CobT, and three methyltransferases, BzaC, BzaD, and BzaE, that conduct three distinct methylation steps. Of these, the methyltransferases that contribute to benzimidazole lower ligand d

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46

Pacifici, G. M., P. Romiti, S. Santerini, and L. Giuliani. "S-methyltransferases in human intestine: differential distribution of the microsomal thiol methyltransferase and cytosolic thiopurine methyltransferase along the human bowel." Xenobiotica 23, no. 6 (1993): 671–79. http://dx.doi.org/10.3109/00498259309059404.

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Zhou, Yangsheng, Debashish Ray, Yiwei Zhao, et al. "Structure and Function of Flavivirus NS5 Methyltransferase." Journal of Virology 81, no. 8 (2007): 3891–903. http://dx.doi.org/10.1128/jvi.02704-06.

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ABSTRACT The plus-strand RNA genome of flavivirus contains a 5′ terminal cap 1 structure (m7GpppAmG). The flaviviruses encode one methyltransferase, located at the N-terminal portion of the NS5 protein, to catalyze both guanine N-7 and ribose 2′-OH methylations during viral cap formation. Representative flavivirus methyltransferases from dengue, yellow fever, and West Nile virus (WNV) sequentially generate GpppA → m7GpppA → m7GpppAm. The 2′-O methylation can be uncoupled from the N-7 methylation, since m7GpppA-RNA can be readily methylated to m7GpppAm-RNA. Despite exhibiting two distinct methy

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48

Lashley, Audrey, Ryan Miller, Stephanie Provenzano, Sara-Alexis Jarecki, Paul Erba, and Vonny Salim. "Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases." Molecules 28, no. 1 (2022): 43. http://dx.doi.org/10.3390/molecules28010043.

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In plants, methylation is a common step in specialized metabolic pathways, leading to a vast diversity of natural products. The methylation of these small molecules is catalyzed by S-adenosyl-l-methionine (SAM)-dependent methyltransferases, which are categorized based on the methyl-accepting atom (O, N, C, S, or Se). These methyltransferases are responsible for the transformation of metabolites involved in plant defense response, pigments, and cell signaling. Plant natural product methyltransferases are part of the Class I methyltransferase-superfamily containing the canonical Rossmann fold. R

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Fuks, F. "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase." Nucleic Acids Research 31, no. 9 (2003): 2305–12. http://dx.doi.org/10.1093/nar/gkg332.

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Wright, Lynda S., Paul J. Bertics, and Frank L. Siegel. "CalmodulinN-Methyltransferase." Journal of Biological Chemistry 271, no. 22 (1996): 12737–43. http://dx.doi.org/10.1074/jbc.271.22.12737.

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