Literature DB >> 22803949

Binding of DNA methyltransferase M.Ecl18kI [corrected] to operator-promoter region decreases its methylating activity.

D V Nikitin1, M L Mokrishcheva, A S Solonin.   

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.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 22803949     DOI: 10.1134/S0006297912030108

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  1 in total

1.  Kinetic Basis of the Bifunctionality of SsoII DNA Methyltransferase.

Authors:  Nadezhda A Timofeyeva; Alexandra Yu Ryazanova; Maxim V Norkin; Tatiana S Oretskaya; Olga S Fedorova; Elena A Kubareva
Journal:  Molecules       Date:  2018-05-16       Impact factor: 4.411

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.