Abstrakt

New DNA methyltransferase M.AgsI produces TTSA(m6A)

V.S.Dedkov, D.A.Gonchar, V.A.Chernukhin, M.A.Abdurashitov, S.G.Udalyeva, L.A.Urumceva, S.Kh.Degtyarev

Agrococcus species 25 DNA was cloned in pUC19 plasmid of Escherichia coli. Cloned DNA fragment contained two Opened Reading Frames with 8 amino acid motives which belonged to amino DNAmethyltransferases. Thus M.AgsI can be the first of subunit adenine-(N6)-DNA methyltransferase. The enzyme was purified from the recombinant strain by chromatography on P-11 Phosphocellulose, Heparin-Sepharose and Hydroxyapatite. M.AgsI specificity was determined by a study of protection of lambda DNAmethylated withM.AgsI against cleavage with some restriction endonucleases.Asensitivity of restriction endonucleases to M.AgsI-methylation was studied.