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Journal articles on the topic 'Adenine Methyltransferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

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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2

Coffin, Stephanie R., and Norbert O. Reich. "Escherichia coliDNA Adenine Methyltransferase." Journal of Biological Chemistry 284, no. 27 (2009): 18390–400. http://dx.doi.org/10.1074/jbc.m109.005876.

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3

Kiss, Antal, Csaba Finta, and Pál Venetianer. "M.Kpnlis an adenine-methyltransferase." Nucleic Acids Research 19, no. 12 (1991): 3460. http://dx.doi.org/10.1093/nar/19.12.3460.

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4

Malygin, Ernst G., Bianca Sclavi, Victor V. Zinoviev, Alexey A. Evdokimov, Stanley Hattman, and Malcolm Buckle. "Bacteriophage T4Dam DNA-(Adenine-N6)-methyltransferase." Journal of Biological Chemistry 279, no. 48 (2004): 50012–18. http://dx.doi.org/10.1074/jbc.m409786200.

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5

Malygin, Ernst G., William M. Lindstrom, Victor V. Zinoviev, et al. "Bacteriophage T4Dam (DNA-(Adenine-N6)-methyltransferase)." Journal of Biological Chemistry 278, no. 43 (2003): 41749–55. http://dx.doi.org/10.1074/jbc.m306397200.

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6

Kossykh, Valeri G., and R. Stephen Lloyd. "A DNA Adenine Methyltransferase of Escherichia coli That Is Cell Cycle Regulated and Essential for Viability." Journal of Bacteriology 186, no. 7 (2004): 2061–67. http://dx.doi.org/10.1128/jb.186.7.2061-2067.2004.

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ABSTRACT DNA sequence analysis revealed that the putative yhdJ DNA methyltransferase gene of Escherichia coli is 55% identical to the Nostoc sp. strain PCC7120 gene encoding DNA methyltransferase AvaIII, which methylates adenine in the recognition sequence, ATGCAT. The yhdJ gene was cloned, and the enzyme was overexpressed and purified. Methylation and restriction analysis showed that the DNA methyltransferase methylates the first adenine in the sequence ATGCAT. This DNA methylation was found to be regulated during the cell cycle, and the DNA adenine methyltransferase was designated M.EcoKCcrM

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7

Konttinen, Olivia, Jason Carmody, Sarath Pathuri, Kyle Anderson, Xiaofeng Zhou, and Norbert Reich. "Cell cycle regulated DNA methyltransferase: fluorescent tracking of a DNA strand-separation mechanism and identification of the responsible protein motif." Nucleic Acids Research 48, no. 20 (2020): 11589–601. http://dx.doi.org/10.1093/nar/gkaa844.

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Abstract DNA adenine methylation by Caulobacter crescentus Cell Cycle Regulated Methyltransferase (CcrM) is an important epigenetic regulator of gene expression. The recent CcrM-DNA cocrystal structure shows the CcrM dimer disrupts four of the five base pairs of the (5′-GANTC-3′) recognition site. We developed a fluorescence-based assay by which Pyrrolo-dC tracks the strand separation event. Placement of Pyrrolo-dC within the DNA recognition site results in a fluorescence increase when CcrM binds. Non-cognate sequences display little to no fluorescence changes, showing that strand separation i

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8

Murray, Iain A., Richard D. Morgan, Yvette Luyten, et al. "The non-specific adenine DNA methyltransferase M.EcoGII." Nucleic Acids Research 46, no. 2 (2017): 840–48. http://dx.doi.org/10.1093/nar/gkx1191.

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9

Aranda, Juan, Kirill Zinovjev, Maite Roca, and Iñaki Tuñón. "Dynamics and Reactivity inThermus aquaticusN6-Adenine Methyltransferase." Journal of the American Chemical Society 136, no. 46 (2014): 16227–39. http://dx.doi.org/10.1021/ja5077124.

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10

Zinoviev, Victor V., Alexey A. Evdokimov, Ernst G. Malygin, Samuel L. Schlagman, and Stanley Hattman. "Bacteriophage T4 Dam DNA-(N6-adenine)-methyltransferase." Journal of Biological Chemistry 278, no. 10 (2002): 7829–33. http://dx.doi.org/10.1074/jbc.m210769200.

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11

Evdokimov, Alexey A., Victor V. Zinoviev, Ernst G. Malygin, Samuel L. Schlagman, and Stanley Hattman. "Bacteriophage T4 Dam DNA-[N6-adenine]Methyltransferase." Journal of Biological Chemistry 277, no. 1 (2001): 279–86. http://dx.doi.org/10.1074/jbc.m108864200.

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12

van Steensel, Bas, Jeffrey Delrow, and Steven Henikoff. "Chromatin profiling using targeted DNA adenine methyltransferase." Nature Genetics 27, no. 3 (2001): 304–8. http://dx.doi.org/10.1038/85871.

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13

Fedoreyeva, Larisa I., and Boris F. Vanyushin. "N6-Adenine DNA-methyltransferase in wheat seedlings." FEBS Letters 514, no. 2-3 (2002): 305–8. http://dx.doi.org/10.1016/s0014-5793(02)02384-0.

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14

Kloor, Doris, Katrin Karnahl, and Jost Kömpf. "Characterization of glycineN-methyltransferase from rabbit liver." Biochemistry and Cell Biology 82, no. 3 (2004): 369–74. http://dx.doi.org/10.1139/o04-007.

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The enzymatic properties of glycine N-methyltransferase from rabbit liver and the effects of endogenous adenosine nucleosides, nucleotides and methyltransferase inhibitors were investigated using a photometrical assay to detect sarcosine with o-dianisidine as a dye. After isolation and purification the denatured enzyme showed a two-banded pattern by SDS–PAGE. The enzyme was highly specific for its substrates with a pH-optimum at pH 8.6. Glycine N-methyltransferase exhibits Michaelis-Menten kinetics for its substrates, S-adenosylmethionine and glycine, respectively. The apparent Kmand Vmaxvalue

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15

Broadbent, Sarah E., Roberto Balbontin, Josep Casadesus, Martin G. Marinus, and Marjan van der Woude. "YhdJ, a Nonessential CcrM-Like DNA Methyltransferase of Escherichia coli and Salmonella enterica." Journal of Bacteriology 189, no. 11 (2007): 4325–27. http://dx.doi.org/10.1128/jb.01854-06.

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ABSTRACT The Caulobacter crescentus DNA adenine methyltransferase CcrM and its homologs in the α-Proteobacteria are essential for viability. CcrM is 34% identical to the yhdJ gene products of Escherichia coli and Salmonella enterica. This study provides evidence that the E. coli yhdJ gene encodes a DNA adenine methyltransferase. In contrast to an earlier report, however, we show that yhdJ is not an essential gene in either E. coli or S. enterica.

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16

Woodcock, Clayton B., John R. Horton, Xing Zhang, Robert M. Blumenthal, and Xiaodong Cheng. "Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences." Nucleic Acids Research 48, no. 18 (2020): 10034–44. http://dx.doi.org/10.1093/nar/gkaa446.

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Abstract S-adenosyl-l-methionine dependent methyltransferases catalyze methyl transfers onto a wide variety of target molecules, including DNA and RNA. We discuss a family of methyltransferases, those that act on the amino groups of adenine or cytosine in DNA, have conserved motifs in a particular order in their amino acid sequence, and are referred to as class beta MTases. Members of this class include M.EcoGII and M.EcoP15I from Escherichia coli, Caulobacter crescentus cell cycle–regulated DNA methyltransferase (CcrM), the MTA1-MTA9 complex from the ciliate Oxytricha, and the mammalian MettL

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17

Zhang, Weiting, Xiaolong Zu, Yanling Song, Zhi Zhu, and Chaoyong James Yang. "Detection of DNA methyltransferase activity using allosteric molecular beacons." Analyst 141, no. 2 (2016): 579–84. http://dx.doi.org/10.1039/c5an01763g.

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Abnormal DNA methylation patterns caused by altered DNA methyltransferase (MTase) activity are closely associated with cancer. Herein, using DNA adenine methylation methyltransferase (Dam MTase) as a model analyte, we designed an allosteric molecular beacon (aMB) for sensitive detection of Dam MTase activity.

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18

Thomas, Chad B., Robert D. Scavetta, Richard I. Gumport, and Mair E. A. Churchill. "Structures of Liganded and UnligandedRsrIN6-Adenine DNA Methyltransferase." Journal of Biological Chemistry 278, no. 28 (2003): 26094–101. http://dx.doi.org/10.1074/jbc.m303751200.

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19

Yang, Zhe, John R. Horton, Lan Zhou, et al. "Structure of the bacteriophage T4 DNA adenine methyltransferase." Nature Structural & Molecular Biology 10, no. 10 (2003): 849–55. http://dx.doi.org/10.1038/nsb973.

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20

Tang, Feng, Xi-Wen Xing, Jie-Mei Chu, et al. "A highly sensitive fluorescence assay for methyltransferase activity by exonuclease-aided signal amplification." Analyst 140, no. 13 (2015): 4636–41. http://dx.doi.org/10.1039/c5an00732a.

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21

Kong, Yimeng, Lei Cao, Gintaras Deikus, et al. "Critical assessment of DNA adenine methylation in eukaryotes using quantitative deconvolution." Science 375, no. 6580 (2022): 515–22. http://dx.doi.org/10.1126/science.abe7489.

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The discovery of N 6 -methyldeoxyadenine (6mA) across eukaryotes led to a search for additional epigenetic mechanisms. However, some studies have highlighted confounding factors that challenge the prevalence of 6mA in eukaryotes. We developed a metagenomic method to quantitatively deconvolve 6mA events from a genomic DNA sample into species of interest, genomic regions, and sources of contamination. Applying this method, we observed high-resolution 6mA deposition in two protozoa. We found that commensal or soil bacteria explained the vast majority of 6mA in insect and plant samples. We found n

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22

Scavetta, R. D. "Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases." Nucleic Acids Research 28, no. 20 (2000): 3950–61. http://dx.doi.org/10.1093/nar/28.20.3950.

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23

Erova, Tatiana E., Lakshmi Pillai, Amin A. Fadl, et al. "DNA Adenine Methyltransferase Influences the Virulence of Aeromonas hydrophila." Infection and Immunity 74, no. 1 (2006): 410–24. http://dx.doi.org/10.1128/iai.74.1.410-424.2006.

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ABSTRACT Among the various virulence factors produced by Aeromonas hydrophila, a type II secretion system (T2SS)-secreted cytotoxic enterotoxin (Act) and the T3SS are crucial in the pathogenesis of Aeromonas-associated infections. Our laboratory molecularly characterized both Act and the T3SS from a diarrheal isolate, SSU of A. hydrophila, and defined the role of some regulatory genes in modulating the biological effects of Act. In this study, we cloned, sequenced, and expressed the DNA adenine methyltransferase gene of A. hydrophila SSU (dam AhSSU) in a T7 promoter-based vector system using E

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24

Yamazaki, Norihiko, Hiroyuki Hori, Kiyoshi Ozawa, et al. "Substrate Specificity of tRNA (Adenine-1-)-methyltransferase fromThermus thermophilusHB27." Bioscience, Biotechnology, and Biochemistry 58, no. 6 (1994): 1128–33. http://dx.doi.org/10.1271/bbb.58.1128.

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25

Hobley, Gerard, Jennifer C. McKelvie, Jenny E. Harmer, Jason Howe, Petra C. F. Oyston, and Peter L. Roach. "Development of rationally designed DNA N6 adenine methyltransferase inhibitors." Bioorganic & Medicinal Chemistry Letters 22, no. 9 (2012): 3079–82. http://dx.doi.org/10.1016/j.bmcl.2012.03.072.

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26

Thomas, C. B. "Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase." Nucleic Acids Research 34, no. 3 (2006): 806–15. http://dx.doi.org/10.1093/nar/gkj486.

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27

Schlagman, Samuel L., Zoe Miner, Zsigmond Fehér, and Stanley Hattman. "The DNA [adenine-N6]methyltransferase (Dam) of bacteriophage T4." Gene 73, no. 2 (1988): 517–30. http://dx.doi.org/10.1016/0378-1119(88)90516-1.

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28

Ashihara, Hiroshi. "Metabolism of alkaloids in coffee plants." Brazilian Journal of Plant Physiology 18, no. 1 (2006): 1–8. http://dx.doi.org/10.1590/s1677-04202006000100001.

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Coffee beans contain two types of alkaloids, caffeine and trigonelline, as major components. This review describes the distribution and metabolism of these compounds. Caffeine is synthesised from xanthosine derived from purine nucleotides. The major biosynthetic route is xanthosine -> 7-methylxanthosine -> 7-methylxanthine -> theobromine -> caffeine. Degradation activity of caffeine in coffee plants is very low, but catabolism of theophylline is always present. Theophylline is converted to xanthine, and then enters the conventional purine degradation pathway. A recent development i

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29

Kumar, Ritesh, and Desirazu N. Rao. "A nucleotide insertion between two adjacent methyltransferases in Helicobacter pylori results in a bifunctional DNA methyltransferase." Biochemical Journal 433, no. 3 (2011): 487–95. http://dx.doi.org/10.1042/bj20101668.

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Helicobacter pylori has a dynamic R-M (restriction–modification) system. It is capable of acquiring new R-M systems from the environment in the form of DNA released from other bacteria or other H. pylori strains. Random mutations in R-M genes can result in non-functional R-M systems or R-M systems with new properties. hpyAVIAM and hpyAVIBM are two solitary DNA MTase (methyltransferase) genes adjacent to each other and lacking a cognate restriction enzyme gene in H. pylori strain 26695. Interestingly, in an Indian strain D27, hpyAVIAM–hpyAVIBM encodes a single bifunctional polypeptide due to in

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30

Liu, Peng, Song Nie, Bing Li, et al. "Deficiency in a Glutamine-Specific Methyltransferase for Release Factor Causes Mouse Embryonic Lethality." Molecular and Cellular Biology 30, no. 17 (2010): 4245–53. http://dx.doi.org/10.1128/mcb.00218-10.

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ABSTRACT Biological methylation is a fundamental enzymatic reaction for a variety of substrates in multiple cellular processes. Mammalian N6amt1 was thought to be a homologue of bacterial N 6-adenine DNA methyltransferases, but its substrate specificity and physiological importance remain elusive. Here, we demonstrate that N6amt1 functions as a protein methyltransferase for the translation termination factor eRF1 in mammalian cells both in vitro and in vivo. Mass spectrometry analysis indicated that about 70% of the endogenous eRF1 is methylated at the glutamine residue of the conserved GGQ mo

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31

Mruk, Iwona, Magdalena Cichowicz, and Tadeusz Kaczorowski. "Characterization of the LlaCI methyltransferase from Lactococcus lactis subsp. cremoris W15 provides new insights into the biology of type II restriction–modification systems." Microbiology 149, no. 11 (2003): 3331–41. http://dx.doi.org/10.1099/mic.0.26562-0.

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The gene encoding the LlaCI methyltransferase (M.LlaCI) from Lactococcus lactis subsp. cremoris W15 was overexpressed in Escherichia coli. The enzyme was purified to apparent homogeneity using three consecutive steps of chromatography on phosphocellulose, blue-agarose and Superose 12HR, yielding a protein of M r 31 300±1000 under denaturing conditions. The exact position of the start codon AUG was determined by protein microsequencing. This enzyme recognizes the specific palindromic sequence 5′-AAGCTT-3′. Purified M.LlaCI was characterized. Unlike many other methyltransferases, M.LlaCI exists

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32

Pollak, Adam J., and Norbert O. Reich. "Proximal Recognition Sites Facilitate Intrasite Hopping by DNA Adenine Methyltransferase." Journal of Biological Chemistry 287, no. 27 (2012): 22873–81. http://dx.doi.org/10.1074/jbc.m111.332502.

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33

Brawer, Rolando, Facundo D. Batista, Oscar R. Burrone, Daniel O. Sordelli, and M. C. Cerquetti. "A temperature-sensitive DNA adenine methyltransferase mutant of Salmonella typhimurium." Archives of Microbiology 169, no. 6 (1998): 530–33. http://dx.doi.org/10.1007/s002030050607.

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34

Bandyopadhyay, Rupa, and Jyotirmoy Das. "The DNA adenine methyltransferase-encoding gene (dam) of Vibrio cholerae." Gene 140, no. 1 (1994): 67–71. http://dx.doi.org/10.1016/0378-1119(94)90732-3.

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35

Mitra, Amitava, and Quideng Que. "Ectopic expression of a viral adenine methyltransferase gene in tobacco." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1219, no. 1 (1994): 244–49. http://dx.doi.org/10.1016/0167-4781(94)90282-8.

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36

Bheemanaik, Shivakumara, Srivani Sistla, Vinita Krishnamurthy, Sampath Arathi, and Narasimha Rao Desirazu. "Kinetics of Methylation by EcoP1I DNA Methyltransferase." Enzyme Research 2010 (July 15, 2010): 1–14. http://dx.doi.org/10.4061/2010/302731.

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EcoP1I DNA MTase (M.EcoP1I), an N6-adenine MTase from bacteriophage P1, is a part of the EcoP1I restriction-modification (R-M) system which belongs to the Type III R-M system. It recognizes the sequence 5'-AGACC-3' and methylates the internal adenine. M.EcoP1I requires Mg2+ for the transfer of methyl groups to DNA. M.EcoP1I is shown to exist as dimer in solution, and even at high salt concentrations (0.5 M) the dimeric M.EcoP1I does not dissociate into monomers suggesting a strong interaction between the monomer subunits. Preincubation and isotope partitioning studies with M.EcoP1I indicate a

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37

Algire, Mikkel A., Michael G. Montague, Sanjay Vashee, Carole Lartigue, and Chuck Merryman. "A Type III restriction–modification system in Mycoplasma mycoides subsp. capri." Open Biology 2, no. 10 (2012): 120115. http://dx.doi.org/10.1098/rsob.120115.

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The sequenced genome of Mycoplasma mycoides subsp. capri revealed the presence of a Type III restriction–modification system (MmyCI). The methyltransferase (modification) subunit of MmyCI (M.MmyCI) was shown to recognize the sequence 5′-TGAG-3′ and methylate the adenine. The coding region of the methyltransferase gene contains 12 consecutive AG dinucleotide repeats that result in a translational termination at a TAA codon immediately beyond the repeat region. This strain does not have MmyCI activity. A clone was found with 10 AG repeats such that the gene is in frame, and this strain has MmyCI

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38

Atkinson, Gemma C., Lykke H. Hansen, Tanel Tenson, Anette Rasmussen, Finn Kirpekar, and Birte Vester. "Distinction between the Cfr Methyltransferase Conferring Antibiotic Resistance and the Housekeeping RlmN Methyltransferase." Antimicrobial Agents and Chemotherapy 57, no. 8 (2013): 4019–26. http://dx.doi.org/10.1128/aac.00448-13.

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ABSTRACTThecfrgene encodes the Cfr methyltransferase that primarily methylates C-8 in A2503 of 23S rRNA in the peptidyl transferase region of bacterial ribosomes. The methylation provides resistance to six classes of antibiotics of clinical and veterinary importance. TherlmNgene encodes the RlmN methyltransferase that methylates C-2 in A2503 in 23S rRNA and A37 in tRNA, but RlmN does not significantly influence antibiotic resistance. The enzymes are homologous and use the same mechanism involving radicalS-adenosyl methionine to methylate RNA via an intermediate involving a methylated cysteine

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39

Sharkey, Rory E., Johnny B. Herbert, Danielle A. McGaha, Vy Nguyen, Allyn J. Schoeffler, and Jack A. Dunkle. "Three critical regions of the erythromycin resistance methyltransferase, ErmE, are required for function supporting a model for the interaction of Erm family enzymes with substrate rRNA." RNA 28, no. 2 (2021): 210–26. http://dx.doi.org/10.1261/rna.078946.121.

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6-Methyladenosine modification of DNA and RNA is widespread throughout the three domains of life and often accomplished by a Rossmann-fold methyltransferase domain which contains conserved sequence elements directing S-adenosylmethionine cofactor binding and placement of the target adenosine residue into the active site. Elaborations to the conserved Rossman-fold and appended domains direct methylation to diverse DNA and RNA sequences and structures. Recently, the first atomic-resolution structure of a ribosomal RNA adenine dimethylase (RRAD) family member bound to rRNA was solved, TFB1M bound

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40

Wu, H., J. E. Lippmann, J. P. Oza, M. Zeng, P. Fives-Taylor, and N. O. Reich. "Inactivation of DNA adenine methyltransferase alters virulence factors in Actinobacillus actinomycetemcomitans." Oral Microbiology and Immunology 21, no. 4 (2006): 238–44. http://dx.doi.org/10.1111/j.1399-302x.2006.00284.x.

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41

Mashhoon, Neda, Michael Carroll, Cynthia Pruss, et al. "Functional Characterization ofEscherichia coliDNA Adenine Methyltransferase, a Novel Target for Antibiotics." Journal of Biological Chemistry 279, no. 50 (2004): 52075–81. http://dx.doi.org/10.1074/jbc.m408182200.

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We have characterizedEscherichia coliDNA adenine methyltransferase, a critical regulator of bacterial virulence. Steady-state kinetics, product inhibition, and isotope exchange studies are consistent with a kinetic mechanism in which the cofactorS-adenosylmethionine binds first, followed by sequence-specific DNA binding and catalysis. The enzyme has a fast methyl transfer step followed by slower product release steps, and we directly demonstrate the competence of the enzyme cofactor complex. Methylation of adjacent GATC sites is distributive with DNA derived from a genetic element that control

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42

Saridaki, Aggeliki, Panagiotis Sapountzis, Harriet L. Harris, et al. "Wolbachia Prophage DNA Adenine Methyltransferase Genes in Different Drosophila-Wolbachia Associations." PLoS ONE 6, no. 5 (2011): e19708. http://dx.doi.org/10.1371/journal.pone.0019708.

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43

Horton, John R., Kirsten Liebert, Miklos Bekes, Albert Jeltsch, and Xiaodong Cheng. "Structure and Substrate Recognition of the Escherichia coli DNA Adenine Methyltransferase." Journal of Molecular Biology 358, no. 2 (2006): 559–70. http://dx.doi.org/10.1016/j.jmb.2006.02.028.

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44

Pouillot, Flavie, Corinne Fayolle, and Elisabeth Carniel. "A putative DNA adenine methyltransferase is involved in Yersinia pseudotuberculosis pathogenicity." Microbiology 153, no. 8 (2007): 2426–34. http://dx.doi.org/10.1099/mic.0.2007/005736-0.

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45

Bochow, S., J. Elliman, and L. Owens. "Bacteriophage adenine methyltransferase: a life cycle regulator? Modelled usingVibrio harveyimyovirus like." Journal of Applied Microbiology 113, no. 5 (2012): 1001–13. http://dx.doi.org/10.1111/j.1365-2672.2012.05358.x.

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46

Dryden, D. T. F., D. F. Willcock, and N. E. Murray. "Mutational analysis of conserved amino-acid motifs in EcoKI adenine methyltransferase." Gene 157, no. 1-2 (1995): 123–24. http://dx.doi.org/10.1016/0378-1119(94)00630-b.

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47

Wachino, Jun-ichi, Keigo Shibayama, Hiroshi Kurokawa, et al. "Novel Plasmid-Mediated 16S rRNA m1A1408 Methyltransferase, NpmA, Found in a Clinically Isolated Escherichia coli Strain Resistant to Structurally Diverse Aminoglycosides." Antimicrobial Agents and Chemotherapy 51, no. 12 (2007): 4401–9. http://dx.doi.org/10.1128/aac.00926-07.

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ABSTRACT We have isolated a multiple-aminoglycoside-resistant Escherichia coli strain, strain ARS3, and have been the first to identify a novel plasmid-mediated 16S rRNA methyltransferase, NpmA. This new enzyme shared a relatively low level of identity (30%) to the chromosomally encoded 16S rRNA methyltransferase (KamA) of Streptomyces tenjimariensis, an actinomycete aminoglycoside producer. The introduction of a recombinant plasmid carrying npmA could confer on E. coli consistent resistance to both 4,6-disubstituted 2-deoxystreptamines, such as amikacin and gentamicin, and 4,5-disubstituted 2

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48

Szegedi, S. S. "Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase." Nucleic Acids Research 28, no. 20 (2000): 3962–71. http://dx.doi.org/10.1093/nar/28.20.3962.

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49

Coffin, Stephanie R., and Norbert O. Reich. "Escherichia coliDNA Adenine Methyltransferase: Intrasite Processivity and Substrate-Induced Dimerization and Activation." Biochemistry 48, no. 31 (2009): 7399–410. http://dx.doi.org/10.1021/bi9008006.

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50

Xia, Yuannan, James L. Van Etten, Peter Dobos, Yuan Yuan Ling, and Peter J. Krell. "Adenine DNA Methyltransferase M.CviRI Expression Accelerates Apoptosis in Baculovirus-Infected Insect Cells." Virology 196, no. 2 (1993): 817–24. http://dx.doi.org/10.1006/viro.1993.1539.

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