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. 1991 Aug 1;88(15):6394–6397. doi: 10.1073/pnas.88.15.6394

Allosteric and catalytic binding of S-adenosylmethionine to Escherichia coli DNA adenine methyltransferase monitored by 3H NMR.

A Bergerat 1, W Guschlbauer 1, G V Fazakerley 1
PMCID: PMC52091  PMID: 1862071

Abstract

Adenine methylation of GATC sequences in DNA is carried out by the DNA adenine methyltransferase with the methyl group source being the cofactor S-adenosylmethionine. We report 3H NMR studies on the interaction of DNA adenine methyltransferase with S-adenosylmethionine and the reaction when the ternary complex is formed with an oligonucleotide containing a GATC site. The methylation reaction was also studied in the presence of a competitive inhibitor and this showed two successive stages involved in the methylation and two sites of binding for S-adenosylmethionine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barras F., Marinus M. G. The great GATC: DNA methylation in E. coli. Trends Genet. 1989 May;5(5):139–143. doi: 10.1016/0168-9525(89)90054-1. [DOI] [PubMed] [Google Scholar]
  2. Bergerat A., Guschlbauer W. The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli. Nucleic Acids Res. 1990 Aug 11;18(15):4369–4375. doi: 10.1093/nar/18.15.4369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  4. Fazakerley G. V., Quignard E., Teoule R., Guy A., Guschlbauer W. A two-dimensional 1H-NMR study of the dam methylase site: comparison between the hemimethylated GATC sequence, its unmethylated analogue and a hemimethylated CATG sequence. The sequence dependence of methylation upon base-pair lifetimes. Eur J Biochem. 1987 Sep 15;167(3):397–404. doi: 10.1111/j.1432-1033.1987.tb13351.x. [DOI] [PubMed] [Google Scholar]
  5. Fazakerley G. V., Téoule R., Guy A., Fritzsche H., Guschlbauer W. NMR studies on oligodeoxyribonucleotides containing the dam methylation site GATC. Comparison between d(GGATCC) and d(GGm6ATCC). Biochemistry. 1985 Aug 13;24(17):4540–4548. doi: 10.1021/bi00338a009. [DOI] [PubMed] [Google Scholar]
  6. Geier G. E., Modrich P. Recognition sequence of the dam methylase of Escherichia coli K12 and mode of cleavage of Dpn I endonuclease. J Biol Chem. 1979 Feb 25;254(4):1408–1413. [PubMed] [Google Scholar]
  7. Hattman S., Brooks J. E., Masurekar M. Sequence specificity of the P1 modification methylase (M.Eco P1) and the DNA methylase (M.Eco dam) controlled by the Escherichia coli dam gene. J Mol Biol. 1978 Dec 15;126(3):367–380. doi: 10.1016/0022-2836(78)90046-3. [DOI] [PubMed] [Google Scholar]
  8. Herman G. E., Modrich P. Escherichia coli dam methylase. Physical and catalytic properties of the homogeneous enzyme. J Biol Chem. 1982 Mar 10;257(5):2605–2612. [PubMed] [Google Scholar]
  9. Messer W., Noyer-Weidner M. Timing and targeting: the biological functions of Dam methylation in E. coli. Cell. 1988 Sep 9;54(6):735–737. doi: 10.1016/s0092-8674(88)90911-7. [DOI] [PubMed] [Google Scholar]
  10. Newmark R. D., Un S., Williams P. G., Carson P. J., Morimoto H., Klein M. P. 3H nuclear magnetic resonance study of anaerobic glycolysis in packed erythrocytes. Proc Natl Acad Sci U S A. 1990 Jan;87(2):583–587. doi: 10.1073/pnas.87.2.583. [DOI] [PMC free article] [PubMed] [Google Scholar]

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