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J. Biol. Chem., Vol. 282, Issue 6, 3520-3530, February 9, 2007

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A Mutation in the Mod Subunit of EcoP15I Restriction Enzyme Converts the DNA Methyltransferase to a Site-specific Endonuclease^*

From the Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India

A closer inspection of the amino acid sequence of EcoP15I DNA methyltransferase revealed a region of similarity to the PDX_n(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.

Received for publication, April 5, 2006 , and in revised form, November 2, 2006.

^* This work was supported by the Department of Biotechnology Program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² Recipient of a senior research fellowship from Council of Scientific and Industrial Research.

³ To whom correspondence should be addressed. Tel.: 91-80-22932538; Fax: 91-80-23600814; E-mail: dnrao{at}biochem.iisc.ernet.in.

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