Abstract
The type II bifunctional DNA methyltransferase (MTase) Ecl18 that is able to control transcription of its own gene was studied kinetically. Based on initial velocity dependences from S-adenosyl-L-methionine (AdoMet) and target DNA and substrate preincubation assays, it is proposed that the enzyme apparently works by a rapid equilibrium ordered bi-bi mechanism with DNA binding first. By measuring the enzyme activity depending on DNA and AdoMet at different fixed concentrations of the operator sequence oligonucleotide, it was found that its binding has noncompetitive inhibitory effect on Ecl18 MTase activity.
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Abbreviations
- AdoMet:
-
S-adenosyl-L-methionine
- DE:
-
diethylaminoethyl
- MTases:
-
DNA methyltransferases
- RE:
-
restriction endonuclease
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Published in Russian in Biokhimiya, 2012, Vol. 77, No. 3, pp. 392–397.
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Nikitin, D.V., Mokrishcheva, M.L. & Solonin, A.S. Binding of DNA methyltransferase M.Ecl18 to operator-promoter region decreases its methylating activity. Biochemistry Moscow 77, 307–311 (2012). https://doi.org/10.1134/S0006297912030108
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DOI: https://doi.org/10.1134/S0006297912030108