The Enzymatic Methylation of Rna and Dna, Ii. On the Species Specificity of the Methylation Enzymes

Gold, Marvin; Hurwitz, Jerard; Anders, Monika

doi:10.1073/pnas.50.1.164

Cited by 93 publications

(43 citation statements)

References 9 publications

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“…Escherichia coli AdoMet-dependent tRNA (m 5 U54) methyltransferase (classical name, RNA uridine methyltransferase) is one of the best-studied tRNA modification enzymes. The enzymatic activity was initially detected in crude E. coli cell extract, after which several purification procedures were developed (17)(18)(19). The gene encoding the enzyme was identified as trmA (20).…”

mentioning

confidence: 99%

The tRNA Recognition Mechanism of Folate/FAD-dependent tRNA Methyltransferase (TrmFO)

Yamagami

Yamashita

Nishimasu

et al. 2012

Journal of Biological Chemistry

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Background: RNA modification enzymes select specific RNAs as substrates. Results: A novel assay for folate-dependent tRNA methyltransferase (TrmFO) was developed that clarified positive and negative determinants of TrmFO. Conclusion: TrmFO recognizes a T-arm structure including the U54U55C56 sequence and G53-C61 base pair; A38 prevents incorrect methylation of U32. Significance: Studying how proteins recognize RNA is crucial for understanding RNA maturation processes.

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confidence: 99%

The tRNA Recognition Mechanism of Folate/FAD-dependent tRNA Methyltransferase (TrmFO)

Yamagami

Yamashita

Nishimasu

et al. 2012

Journal of Biological Chemistry

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“…All of the guanine deaminases reported here act over a broad pH range (Table 2). Therefore all enzymatic reactions were carried out at pH 7.5. In contrast to the guanine deaminases of the trypanosomid flagellates, rabbit liver guanase, assayed at pH 8.0, was not sensitive to 6 (4). Methylation occurs at the polymer level (6,(11)(12)(13)22).…”

Section: Resultsmentioning

confidence: 99%

“…The occurrence of small amounts of 6-MA in the deoxyribonucleic acid (DNA) and transfer RNA (tRNA) of bacteria, plants, and animals is well documented (2,14,23). Enzymes that synthesize these minor bases have been isolated and have been shown to catalyze transfer of the methyl group from S-adenosylmethionine to the appropriate nucleotide residues of the DNA and RNA polymers (6,(11)(12)(13)22).…”

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confidence: 99%

Inhibition of growth and purine-metabolizing enzymes of trypanosomid flagellates by N6-methyladenine

Nolan¹,

Kidder²

1980

Antimicrob Agents Chemother

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N6-methyladenine (6-methylaminopurine [6-MA]), a plant growth regulator and a normal constituent of nucleic acids, has been found to inhibit the growth of Trypanosoma cruzi, Leishmania braziliensis, L. donovani, L. tarentolae, L. mexicana, and Crithidia fasciculata. The extent of growth inhibition in these organisms is related to the sensitivity of guanine deaminase (guanine aminohydrolase, EC 3.5.4.3), adenine deaminase (adenine aminohydrolase, EC 3.5.4.2), and adenosine hydrolase and phosphorylase. 6-MA was not an inhibitor of the purine phosphoribosyltransferases. Of the trypanosomid flagellates tested. Trypanosoma cruzi was most susceptible to 6-MA. Neither adenine deaminase (as found in the leishmaniae and C. fasciculata) nor adenosine deaminase (as found in mammalian cells) could be demonstrated in T. cruzi. Guanine deaminase, which is strikingly inhibited by 6-MA in T. cruzi, appears to play a major role in the purine salvage pathway of this organism, as judged from growth experiments and enzyme inhibition studies. Enzyme sensitivities to 6-MA vary greatly depending upon the organism. Rabbit liver guanine deaminase was shown to be insensitive to 6-MA at the concentrations used in this study.

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“…Each enzyme has a definite base specificity. An earlier paper describes five of these enzymes in more detail: two methylate guanine at N 11 one converts uracil to thymine, one methylates cystosine, and one produces 2-methyladenine and 6-methyl-and 6-dimethylaminopurine from adenine (248). The enzymes do not methylate their homologous transfer RNA in vitro but do methylate heterologous transfer RNA and the synthetic products of RNA polymerase (194a).…”

Section: Nucleic Acid Methylasesmentioning

confidence: 97%

Metabolism of Nucleic Acids (Macromolecular DNA and RNA)

Elson¹

1965

Annu. Rev. Biochem.

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Since it is manifestly impossible to cover the entire field of nucleic acid metabolism in one article, I have restricted this review to recent work on enzymes which have to do with macromolecular nucleic acids. Sections are included on the synthetic enzymes DNA polymerase and RNA polymerase and on enzymes which alter the nucleic acids in their macromolecular state, namely, the DNA and RNA methylases. The concluding section deals with degradative enzymes, chiefly RNase, DNase, and polynucleotide phosphoryl ase, but in a much more cursory manner. The review is based on an exten sive, but certainly not complete, coverage of the recent literature. References 1 through 10 are reviews, books, special collections of articles, and critical papers which deal with various aspects of the subject matter of this review. ENZYMES WHICH SYNTHESIZE NUCLEIC ACIDSThe DNA polymerases and RNA polymerases catalyze the synthesis of polynucleotides by the complementary copying of pre-existing polynucleo tides. The precursors are the appropriate nucleoside triphosphates, and a bivalent cation is required (11-16). During the period under review, there have appeared no serious reasons to doubt that these are the principal, and quite possibly the only, enzymes which catalyze the synthesis de novo of DNA and RNA in nature. Beyond this, a great deal remains to be eluci dated, and much of the recent work has dealt with such matters as the chem ical and physical nature of the polynucleotide templates or primers and prod ucts, details of the reaction mechanisms, differences between the reactions in vivo and in vitro, the association of the enzymes with other cell components, and so forth.DNA POLYMERASEThe location of DNA polymerase in the cell.-In bacterial extracts DNA polymerase has been observed to sediment together with DNA (e.g., 17, 18) . In higher organisms, however, a number of studies had indicated that the enzyme is actually located outside the cell nucleus. In view of the unexpected nature of these findings, the matter has been pursued in several laboratories; and reports have now appeared which provide evidence that at least some of

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The Enzymatic Methylation of Rna and Dna, Ii. On the Species Specificity of the Methylation Enzymes

Cited by 93 publications

References 9 publications

The tRNA Recognition Mechanism of Folate/FAD-dependent tRNA Methyltransferase (TrmFO)

The tRNA Recognition Mechanism of Folate/FAD-dependent tRNA Methyltransferase (TrmFO)

Inhibition of growth and purine-metabolizing enzymes of trypanosomid flagellates by N6-methyladenine

Metabolism of Nucleic Acids (Macromolecular DNA and RNA)

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