Binding of DNA methyltransferase M.Ecl18kI [corrected] to operator-promoter region decreases its methylating activity.
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.
Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. dvnikitin@rambler.ru
D V
DV
Nikitin
M L
ML
Mokrishcheva
A S
AS
Solonin
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D015257:DNA-Cytosine Methylases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008745:Methylation; D009875:Operator Regions, Genetic; D011401:Promoter Regions, Genetic; D012436:S-Adenosylmethionine / Q000378:metabolism
D001426:Bacterial Proteins; D012436:S-Adenosylmethionine; D004247:DNA; D015257:DNA-Cytosine Methylases; C114637:Ecl18kI methyltransferase