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Nucleic Acids Research, 1993, Vol. 21, No. 21 4929-4935
© 1993

ENZYMOLOGY

Substrate recognition and selectivity in the type IC DNA modification methylase M.EcoR124l

Ian Taylor, Damian Watts and Geoff Kneale*

Biophysics Laboratories, School of Biological Sciences, University of Portsmouth , Portsmouth PO1 2DT, UK

*To whom correspondence should be addressed

Received July 15, 1993. Revised September 20, 1993. Accepted September 20, 1993.

The type I DNA modification methylase M.EcoR124l binds sequence specifically to DNA and protects a 25bp fragment containing its cognate recognition sequence from digestion by exonuclease III. Using modified synthetic oligonucleotide duplexeswe have investigated the catalytic properties of the methylase, and have established that a specific adenine on each strand of DNA is the site of methylation. We show that the rate of methylation of each adenine is increased at least 100 fold by prior methylation at the other site. However, this is accompanied by a significant decrease in the affinity of the methylase for these substrates according to competitive gel retardation assays. In contrast, methylation of an adenine in the recognition site which is not a target for the enzyme results in only a small decrease in both DNA binding affinity and rate of methylation by the enzyme.


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