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Originally published In Press as doi:10.1074/jbc.M111625200 on February 4, 2002

J. Biol. Chem., Vol. 277, Issue 16, 14306-14314, April 19, 2002
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Evolutionary Relationship between Different Subgroups of Restriction Endonucleases*

Vera PingoudDagger §, Elena Kubareva, Gudrun StengelDagger , Peter FriedhoffDagger , Janusz M. Bujnicki||, Claus Urbanke**, Anna Sudina, and Alfred PingoudDagger

From the Dagger  Institut für Biochemie, Justus-Liebig-Universität, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany,  A. N. Belozersky Institute, Physicochemical Biology and Chemistry Department, Moscow State University, Moscow 119899, Russia, || Bioinformatics Laboratory, International Institute of Molecular and Cell Biology, 4 Ks. Trojdena, 02-109 Warsaw, Poland, and ** Biophysikalisch-Biochemische Verfahren, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, D-30623 Hannover, Germany

The type II restriction endonuclease SsoII shows sequence similarity with 10 other restriction endonucleases, among them the type IIE restriction endonuclease EcoRII, which requires binding to an effector site for efficient DNA cleavage, and the type IIF restriction endonuclease NgoMIV, which is active as a homotetramer and cleaves DNA with two recognition sites in a concerted reaction. We show here that SsoII is an orthodox type II enzyme, which is active as a homodimer and does not require activation by binding to an effector site. Nevertheless, it shares with EcoRII and NgoMIV a very similar DNA-binding site and catalytic center as shown here by a mutational analysis, indicative of an evolutionary relationship between these three enzymes. We suggest that a similar relationship exists between other orthodox type II, type IIE, and type IIF restriction endonucleases. This may explain why similarities may be more pronounced between members of different subtypes of restriction enzymes than among the members of a given subtype.

* This work was supported by the Deutsche Forschungsgemeinschaft Grant Pi 122/13-3, the Fonds der Chemischen Industrie, and the Deutscher Akademischer Austauschdienst.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Institut für Biochemie, Justus-Liebig-Universität, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany. Tel.: 49-641-99-35402; Fax.: 49-641-99-35409; E-mail: vera.pingoud@chemie.bio.uni-giessen.de.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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