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Relevant bibliographies by topics / Methyltransferase

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Academic literature on the topic 'Methyltransferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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Journal articles on the topic "Methyltransferase"

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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Methyltransferase"

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Vidgren, Jukka. "Crystallographic studies on drug receptors catechol O-methyltransferase and carbonic anhydrase /." Lund : Dept. of Molecular Biophysics, Lund University, 1994. http://catalog.hathitrust.org/api/volumes/oclc/39725795.html.

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Bonnist, Eleanor Y. M. "The investigation of DNA-methyltransferase interactions in the adenine methyltransferases using the time-resolved fluorescence of 2-aminopurine." Thesis, University of Edinburgh, 2008. http://hdl.handle.net/1842/3175.

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The time-resolved fluorescence of 2-aminopurine (2AP) has been used to investigate DNA base flipping by the adenine methyltransferases and to study aspects of the DNA-enzyme interaction. 2AP is an excellent fluorophore to probe base flipping in the adenine methyltransferases because, as demonstrated in the present work on M.TaqI, the 2AP is delivered into the same position inside the enzyme as the natural target adenine and with the same orientation that prepares the adenine for enzyme catalysis. 2AP emits two types of fluorescence when in DNA. The first is the well-known 370-nm emission, whic

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

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For many enzymes to function correctly they must have the freedom to display a level of dynamics or communication during their catalytic cycle. The effects that protein dynamics and communication can have are wide ranging, from changes in substrate specificity or product profiles, to speed of reaction or switching activity on or off. This project investigates the protein dynamics and communication in two separate systems, a non-ribosomal peptide synthetase (NRPS), and a protein arginine methyltransferase (PRMT). PRMT1, the enzyme responsible for 80% of arginine methylation in humans, has been

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Deng, Jing. "Multiple isoforms of rat DNA methyltransferase are encoded by the cytosine DNA methyltransferase gene and differentially expressed." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0020/NQ55320.pdf.

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Deng, Jing 1966. "Multiple isoforms of rat DNA methyltransferase are encoded by the cytosine DNA methyltransferase gene and differentially expressed." Thesis, McGill University, 1999. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=36001.

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Tissue- and gene-specific DNA methylation patterns are hallmarks of vertebrate genomes and have been suggested to play a critical role in regulating genome functions. There is remarkable diversity of DNA methylation patterns. However, it is yet unclear what is responsible for this diversity.<br>In this dissertation, Chapters Two and Three, we test the hypothesis that multiple forms of DNA (cytosine-5) methyltransferase are generated from a single DNA methyltransferase gene (Dnmt1) in vertebrates in vivo. We show that diversification of the N-terminus of Dnmt1 occurs by two mechanisms, multiple

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Frauer, Carina. "Studies of mechanisms controlling DNA methyltransferase 1." Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-121294.

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Lanouette, Sylvain. "Characterization of the Protein Lysine Methyltransferase SMYD2." Thesis, Université d'Ottawa / University of Ottawa, 2015. http://hdl.handle.net/10393/32467.

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Our understanding of protein lysine methyltransferases and their substrates remains limited despite their importance as regulators of the proteome. The SMYD (SET and MYND domain) methyltransferase family plays pivotal roles in various cellular processes, including transcriptional regulation and embryonic development. Among them, SMYD2 is associated with oesophageal squamous cell carcinoma, bladder cancer and leukemia as well as with embryonic development. Initially identified as a histone methyltransferase, SMYD2 was later reported to methylate p53, the retinoblastoma protein pRb and the estro

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Jue, Kathleen. "Regulation of DNA methyltransferase expression during spermatogenesis." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=22746.

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Patterns of methylation at the 5-position of cytosine are postulated to be involved in several mammalian processes such as the regulation of gene expression, genomic imprinting and X chromosome inactivation. Disruptions in methylation patterns affect embryonic development and are involved in carcinogenesis, indicating the importance of regulating these patterns. The establishment of methylation patterns is believed to be initiated during gametogenesis and continue during early embryonic development. DNA (cytosine-5)-methyltransferase (EC2.1.1.37) (DNA methyltransferase) is the only known mamma

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Farrell, Sarah Marie. "The magnetoencephalographic signature of catechol-O-methyltransferase." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:bb375074-7912-4f8b-b123-975dff7d88e0.

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Catechol-O-methyltransferase (COMT) metabolizes catechols, notably dopamine. The COMT Val158Met polymorphism influences its enzyme activity, and multiple neural correlates of this genotype on dopaminergic phenotypes have been reported, particularly with regards to working memory. COMT activity can also be regulated pharmacologically by COMT inhibitors. The ‘inverted-U’ relationship between dopamine signalling and cognitive performance predicts that the effects of COMT inhibition will differ according to COMT genotype. The goal of this thesis was to better understand COMT’s impact on brain func

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McKelvie, Jennifer C. "Novel antibiotics from DNA adenine methyltransferase inhibitors." Thesis, University of Southampton, 2011. https://eprints.soton.ac.uk/341769/.

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The re-emergence of plague as a world-wide health concern and the potential risk posed by bioterrorism has led to an increased interest in available treatments for the disease. The bacterial DNA adenine-N6 methyltransferase, Dam, is involved in the regulation of a range of pathogenic bacteria and has been validated as a target for the development of antimicrobial agents with activity against Yersinia pestis, the causative agent of plague. The lack of a functionally similar enzyme in mammals suggests that highly selective Dam inhibitors could be developed. A coupled, real-time break light Dam a

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Books on the topic "Methyltransferase"

1

Leo, Colleen M. Thiopurine methyltransferase pharmacogenetics. National Library of Canada = Bibliothèque nationale du Canada, 1992.

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2

Fitzpatrick, Teresa. Studies on the serine hydroxymethyltransferase catalysed exchange of the [alpha]-protons of amino acids. University College Dublin, 1998.

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Csaszar, Julika. Katabolismus des Molybdän-Cofaktors: Identifikation der endogenen Thiopterin-Methyltransferase. s.n.], 2014.

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4

Levac, Dylan. The Catharanthus roseus 16-hydroxytabersonine O-methyltransferase involved in vindoline biosynthesis. Brock University, Dept. of Biological Sciences, 2008.

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Gill, Kathryn Anne. Huaman liver nicotinamide-N-Methyltransferase: Population studies and enzyme partial purification. University of Birmingham, 1995.

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6

Yarychkivska, Olga. Biology of maintenance and de novo methylation mediated by DNA methyltransferase-1. [publisher not identified], 2017.

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7

Marks, Philip M. H. Expression, purification and characterisation of the novel type 1 1/2 methyltransferase M.AhdI. University of Portsmouth, Institute of Biomedical and Biomolecular Sciences, 2002.

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Margueron, Raphaël, and Daniel Holoch, eds. Histone Methyltransferases. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4.

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9

G, Clarke Steven, and Tamanoi Fuyuhiko, eds. Protein methyltransferases. Academic Press, 2006.

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10

Pakusch, Anne-Elisabeth. S-Adenosyl-L-methionin:trans-Kaffeoyl-CoA 3-O-Methyltransferase, ein ungewöhnliches Enzym der pflanzlichen Abwehr: Molekulare Charakterisierung und Regulation. [s.n.], 1991.

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Book chapters on the topic "Methyltransferase"

1

Melideo, Scott L., Jun Yong Ha, and Jeffry B. Stock. "Leucine Carboxyl Methyltransferase." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101594.

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Schomburg, Dietmar, and Ida Schomburg. "demethylmenaquinone methyltransferase 2.1.1.163." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_1.

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Arnemann, J. "DNA-Methyltransferase (DNMT)." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3463.

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Jurkowska, Renata Z., Alexandre Ceccaldi, Yingying Zhang, Paola B. Arimondo, and Albert Jeltsch. "DNA Methyltransferase Assays." In Methods in Molecular Biology. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-316-5_13.

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Simola, Nicola, Micaela Morelli, Tooru Mizuno, et al. "DNA Methyltransferase Inhibitors." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1245.

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Schomburg, Dietmar, and Dörte Stephan. "Nicotinamide N-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_1.

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Schomburg, Dietmar, and Dörte Stephan. "Homocysteine S-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_10.

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Schomburg, Dietmar, and Dörte Stephan. "Anthranilate N-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_107.

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Schomburg, Dietmar, and Dörte Stephan. "Methionine S-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_12.

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Schomburg, Dietmar, and Dörte Stephan. "Phosphatidylethanolamine N-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_17.

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Conference papers on the topic "Methyltransferase"

1

Dhanak, Dashyant. "Abstract SY02-02: Inhibition of methyltransferase EZH2." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-sy02-02.

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Mitchell, Khadijah A., Hariharan Easwaran, and Stephen B. Baylin. "Abstract 4779: DNMT3B (a de novo DNA methyltransferase) epigenetically regulates gene expression, independent of its DNA methyltransferase activity." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4779.

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Leitner, K., V. Wieser, I. Tsibulak, et al. "Die Expression der Histon-Methyltransferase EZH2 beim Ovarialkarziom." In Kongressabstracts zur Wissenschaftlichen Tagung der Arbeitsgemeinschaft für gynäkologische Onkologie (AGO) der Österreichischen Gesellschaft für Gynäkologie und Geburtshilfe (OEGGG). Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3403392.

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Jiráček, Jiří, Michaela Collinsová, Ivan Rosenberg, Hana Netušilová, Miloš Buděšínský, and Timothy A. Garrow. "New inhibitors of human betaine-homocysteine S-methyltransferase." In IXth Conference Biologically Active Peptides. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2005. http://dx.doi.org/10.1135/css200508033.

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Liu, Qiong, Hao Geng, Changhui Xue, Tomasz M. Beer, and David Z. Qian. "Abstract 458: Regulation of HIF1a by Set9 lysine methyltransferase." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-458.

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Dahal, Ujwal, Kang Le, and Mamta Gupta. "Abstract 3323: Role of RNA methyltransferase METTL3 in melanoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3323.

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Huimin Deng, Si Ying Png, and Zhiqiang Gao. "DNA methyltransferase activity detection using the personal glucose meter." In 2015 9th International Conference on Sensing Technology (ICST). IEEE, 2015. http://dx.doi.org/10.1109/icsenst.2015.7438359.

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Chahal, Manik, Siham Sabri, Yaoxian Xu, Konrad Famulski, David Murray, and Bassam Abdulkarim. "Abstract 1290: O6-methylguanine-methyltransferase modulates glioblastoma angiogenesis and invasion." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1290.

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Marnolia, A., E. P. Toepak, S. Siregar, D. Kerami, and U. S. F. Tambunan. "Computational screening of flavonoid based inhibitor targeting DENV NS5 methyltransferase." In PROCEEDINGS OF THE 3RD INTERNATIONAL SYMPOSIUM ON CURRENT PROGRESS IN MATHEMATICS AND SCIENCES 2017 (ISCPMS2017). Author(s), 2018. http://dx.doi.org/10.1063/1.5064067.

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

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Reports on the topic "Methyltransferase"

1

Zifeng, Li. Meta analysis of correlation between DNA methyltransferase and SLE disease activity index. INPLASY - International Platform of Registered Systematic Review Protocols, 2020. http://dx.doi.org/10.37766/inplasy2020.4.0004.

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Ren, Ruibao. Effects of Inactivating Ras-Converting Enzyme or Isoprenylcysteine Carboxyl Methyltransferase in the Pathogenesis of Chronic Myelogenous Leukemia. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada486034.

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Meiri, Noam, Michael D. Denbow, and Cynthia J. Denbow. Epigenetic Adaptation: The Regulatory Mechanisms of Hypothalamic Plasticity that Determine Stress-Response Set Point. United States Department of Agriculture, 2013. http://dx.doi.org/10.32747/2013.7593396.bard.

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Our hypothesis was that postnatal stress exposure or sensory input alters brain activity, which induces acetylation and/or methylation on lysine residues of histone 3 and alters methylation levels in the promoter regions of stress-related genes, ultimately resulting in long-lasting changes in the stress-response set point. Therefore, the objectives of the proposal were: 1. To identify the levels of total histone 3 acetylation and different levels of methylation on lysine 9 and/or 14 during both heat and feed stress and challenge. 2. To evaluate the methylation and acetylation levels of histone

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