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Nucleic Acids Research, 1985, Vol. 13, No. 24 8983-8998
© 1985

Articles

Interaction of EcoRII restriction and modification enzymes with synthetic DNA fragments. VI. The binding and cleavage of substrates containing nucleotide analogs

A.A. Yolov, M.N. Vinogradova, E.S. Gromova, A. Rosenthal3, D. Cech3, V.P. Veiko1, V.G. Metelev1, V.G. Kosykh1, Ya.I. Buryanov2, A.A. Bayev2 and Z.A. Shabarova

Department of Chemistry, Moscow State University Moscow 119899 1A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University Moscow 119899 2Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences 142292 Pushchino Moscow Region USSR 3Department of Chemistry, Humboldt University Berlin 1040, GDR

Received August 15, 1985. Revised November 26, 1985. Accepted November 26, 1985.

The present study deals with the binding and cleavage by EcoRII endonuclease of concatemer DNA duplexes containing EcoRII recognition sites Formula in which dT is replaced by dU or 5-bromodeoxyuridine, or 5{downarrow}-terminal dC in the dT-con-taining strand is methylated at position 5. The enzyme molecule is found to interact with the methyl group of the dT residue of the DNA recognition site and to be at least in proximity to the H5 atom of the 5'-terminal dC residue in dT-containing strand of this site. Modification of any of these positions exerts an equal effects on the cleavage of both DNA strands. Endonuclease EcoRII was found to bind the substrate specifically. At the same time modification of the bases in recognized sequence may result in the formation of unproductive, though stable, enzyme-substrate complexes.


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