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Nucleic Acids Research, 2001, Vol. 29, No. 18 3728-3741
© 2001 Oxford University Press

Survey and Summary

Nucleoside triphosphate-dependent restriction enzymes

D. T. F. Dryden*, Noreen E. Murray1 and D. N. Rao2

Department of Chemistry, University of Edinburgh, Joseph Black Building, The King’s Buildings, Mayfield Road, Edinburgh EH9 3JJ, UK, 1Institute of Cell and Molecular Biology, University of Edinburgh, Darwin Building, The King’s Buildings, Mayfield Road, Edinburgh EH9 3JR, UK and 2Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India

The known nucleoside triphosphate-dependent restriction enzymes are hetero-oligomeric proteins that behave as molecular machines in response to their target sequences. They translocate DNA in a process dependent on the hydrolysis of a nucleoside triphosphate. For the ATP-dependent type I and type III restriction and modification systems, the collision of translocating complexes triggers hydrolysis of phosphodiester bonds in unmodified DNA to generate double-strand breaks. Type I endonucleases break the DNA at unspecified sequences remote from the target sequence, type III endonucleases at a fixed position close to the target sequence. Type I and type III restriction and modification (R-M) systems are notable for effective post-translational control of their endonuclease activity. For some type I enzymes, this control is mediated by proteolytic degradation of that subunit of the complex which is essential for DNA translocation and breakage. This control, lacking in the well-studied type II R-M systems, provides extraordinarily effective protection of resident DNA should it acquire unmodified target sequences. The only well-documented GTP-dependent restriction enzyme, McrBC, requires methylated target sequences for the initiation of phosphodiester bond cleavage.

* To whom correspondence should be addressed. Tel: +44 131 650 4735; Fax: +44 131 650 6453; Email: david.dryden{at}ed.ac.uk


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