Biopolym. Cell. 1989; 5(1):22-27.
Structure and Function of Biopolymers
The significance of internucleotide phosphates and noncomplementary substitutions in the oligonucleotide substrates on the interaction with the DNA methylase ecodam
- All-Union Research Institute of Molecular Biology
Koltsovo, Novosibirsk Region, USSR - Institute of Biochemistry and Physiology of Microorganisms, Academy of Sciences of the USSR
Pushchino, Moscow Region, USSR
Abstract
Eco dam methylase is investigated for its interaction with different synthetic oligonucleotide substrates containing some defects in the GATC sequence. The defects are as follows: the absence of one or several nucleotide residues, the presence of 3'-phosphate residue with CHa-S-group, noncomplementary substitution of Ade by Gua or of Gua for Ade in the recognition site of methylase Eco dam. The presence of the 3'S-methyl thiophosphate residue has no essential effect on the methylation of oligonucleotide complexes as compared to the analogous complexes lacking internucleotide phosphate. The introduction of the noncomplementary base pair in the recognition site results in the loss of substrate properties of such imperfect duplexes.
Full text: (PDF, in Russian)
References
[1]
Geier GE, Modrich P. Recognition sequence of the dam methylase of Escherichia coli K12 and mode of cleavage of Dpn I endonuclease. J Biol Chem. 1979;254(4):1408-13.
[2]
Hattman S, Brooks JE, 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;126(3):367-80.
[3]
Bur'ianov IaI, Zakharenko VN, Baev AA. Isolation, purification and properties of adenine DNA methylase Eco dam. Dokl Akad Nauk SSSR. 1981;259(6):1492-5.
[4]
Zinov'ev VV, Gorbunov IuA, Popov SG, Malygin EG, Bur'ianov IaI. Effect of Ecodam DNA-methylase on single-stranded sequences and synthetic oligonucleotides. Mol Biol (Mosk). 1985;19(4):947-54.
[5]
Buryanov YaI, Zinoviev VV, Vienozhinskis MT, Malygin EG, Nesterenko VF, Popov SG, Gorbunov YuA. Does the DNA methylase Eco dam pair nucleotide sequences to form site-specific duplexes? FEBS Lett. 1984;168(1):166-8.
[6]
Hirose T, Crea R, Itakura K. Rapid synthesis of trideoxyribonucleotide blocks. Tetrahedron Lett. 1978;19(28):2449–52.
[7]
Reese CB, Yau L. O-aryl S-methyl phosphorochloridothioates: terminal phosphorylating agents in the phosphotriester approach to oligonucleotide synthesis. J Chem Soc, Chem Commun. 1978;(23):1050-2.
[8]
Brooks JE, Blumenthal RM, Gingeras TR. The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene. Nucleic Acids Res. 1983;11(3):837-51.
[9]
Herman GE, Modrich P. Escherichia coli dam methylase. Physical and catalytic properties of the homogeneous enzyme. J Biol Chem. 1982;257(5):2605-12.
[10]
Tuzikov FV, Zinov'ev VV, Iashina LN, Vavilin VI, Gorbunov IuA. Study of the substrate-induced changes in the state of Eco dam methylase using a method of small-angle x-ray scattering. Mol Biol (Mosk). 1986;20(4):1002-7.
[11]
Rechkunova N. I., Zinoviev V. V., Malygin E. G., Gorbunov Yu. A., Popov S. G., Nesterenko V. F., Buriyanov Ya. I. Dimerization of EcoDam-methylase induced by the oligonucleotide substrate. Biopolym. Cell. 1987; 3(3):152-154