Bist Pradeep, Madhusoodanan Urulangodi Kunhiraman, Rao Desirazu N
Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India.
J Biol Chem. 2007 Feb 9;282(6):3520-30. doi: 10.1074/jbc.M603250200. Epub 2006 Dec 4.
A closer inspection of the amino acid sequence of EcoP15I DNA methyltransferase revealed a region of similarity to the PDXn(D/E)XK catalytic site of type II restriction endonucleases, except for methionine in EcoP15I DNA methyltransferase instead of proline. Substitution of methionine at position 357 by proline converts EcoP15I DNA methyltransferase to a site-specific endonuclease. EcoP15I-M357P DNA methyltransferase specifically binds to the recognition sequence 5'-CAGCAG-3' and cleaves DNA asymmetrically EcoP151-M357P.DNA methyltransferase specifically binds to the recognition sequence 5'-CAGCAG-3' and cleaves DNA asymmetrically, 5'-CAGCAG(N)(10)-3', as indicated by the arrows, in presence of magnesium ions.