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Extent of equilibrium perturbation of the DNA helix upon enzymatic methylation of adenine residues.

Publication ,  Journal Article
Cheng, SC; Herman, G; Modrich, P
Published in: J Biol Chem
January 10, 1985

The extent of equilibrium perturbation of the DNA helix associated with enzymatic methylation of dA residues has been determined by the agarose gel electrophoresis band-shift method. Utilization of EcoRI methylase under conditions of reduced specificity together with Escherichia coli dam methylase permitted modification of up to 300 dA residues/plasmid pBR322 dimer. A conformational change associated with methylation was observed, with the magnitude of the transition being linear with extent of modification of relaxed DNA circles. The conformational change corresponds to an unwinding of the DNA helix by 0.5 degrees/methyl group transferred to relaxed molecules. The magnitude of the effect was independent of temperature from 5-37 degrees C indicating that it is not the consequence of a thermal transition within this range.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

January 10, 1985

Volume

260

Issue

1

Start / End Page

191 / 194

Location

United States

Related Subject Headings

  • Thermodynamics
  • Site-Specific DNA-Methyltransferase (Adenine-Specific)
  • Plasmids
  • Nucleic Acid Conformation
  • Methyltransferases
  • Methylation
  • Kinetics
  • Escherichia coli
  • DNA
  • Biochemistry & Molecular Biology
 

Citation

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Cheng, S. C., Herman, G., & Modrich, P. (1985). Extent of equilibrium perturbation of the DNA helix upon enzymatic methylation of adenine residues. J Biol Chem, 260(1), 191–194.
Cheng, S. C., G. Herman, and P. Modrich. “Extent of equilibrium perturbation of the DNA helix upon enzymatic methylation of adenine residues.J Biol Chem 260, no. 1 (January 10, 1985): 191–94.
Cheng SC, Herman G, Modrich P. Extent of equilibrium perturbation of the DNA helix upon enzymatic methylation of adenine residues. J Biol Chem. 1985 Jan 10;260(1):191–4.
Cheng, S. C., et al. “Extent of equilibrium perturbation of the DNA helix upon enzymatic methylation of adenine residues.J Biol Chem, vol. 260, no. 1, Jan. 1985, pp. 191–94.
Cheng SC, Herman G, Modrich P. Extent of equilibrium perturbation of the DNA helix upon enzymatic methylation of adenine residues. J Biol Chem. 1985 Jan 10;260(1):191–194.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

January 10, 1985

Volume

260

Issue

1

Start / End Page

191 / 194

Location

United States

Related Subject Headings

  • Thermodynamics
  • Site-Specific DNA-Methyltransferase (Adenine-Specific)
  • Plasmids
  • Nucleic Acid Conformation
  • Methyltransferases
  • Methylation
  • Kinetics
  • Escherichia coli
  • DNA
  • Biochemistry & Molecular Biology