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Restriction Endonucleases pp 339–360Cite as

Role of Metal Ions in Promoting DNA Binding and Cleavage by Restriction Endonucleases

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Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC,volume 14))

Abstract

While three major classes of restriction endonucleases have been identified (Types I, II, and III), Type II are the most straightforward inasmuch as they require divalent magnesium as an essential cofactor but have no need for ATP (Stasiak 1980; Bennett and Halford 1989; Bujnicki 2000; Murray 2000; Sapranauskas et al. 2000; Pingoud and Jeltsch 2001). A complete classification of Type II restriction nucleases has been presented elsewhere (Pingoud and Jeltsch 2001) and the family is noted for the remarkable specificity and simplicity of its function. These enzymes cleave both strands of doublestrand DNA either at or near a recognition sequence that tends to be palindromic. Consequently most restriction endonucleases are dimeric and recognize symmetric DNA sequences. While showing many functional similarities in DNA recognition and catalytic cleavage, restriction endonucleases also display low sequence homology, and diversity in mechanisms of recognizing DNA target sequences and the positioning of metal cofactors (Aggarwal 1995; Wah et al. 1997; Viadiu and Aggarwal 1998). Such diversity results in subtle variations in both protein binding locations and potential functional roles for essential metal cofactors that are only now coming under investigation.

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  1. Evans Laboratory of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio, 43210, USA

    J. A. Cowan

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  1. Institute for Biochemistry, Justus-Liebig-University, Heinrich-Buff-Ring 58, 35392, Giessen, Germany

    Alfred M. Pingoud

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© 2004 Springer-Verlag Berlin Heidelberg

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Cowan, J.A. (2004). Role of Metal Ions in Promoting DNA Binding and Cleavage by Restriction Endonucleases. In: Pingoud, A.M. (eds) Restriction Endonucleases. Nucleic Acids and Molecular Biology, vol 14. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18851-0_13

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  • DOI: https://doi.org/10.1007/978-3-642-18851-0_13

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