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. 1993 Oct 25;21(21):4929–4935. doi: 10.1093/nar/21.21.4929

Substrate recognition and selectivity in the type IC DNA modification methylase M.EcoR124I.

I Taylor 1, D Watts 1, G Kneale 1
PMCID: PMC311408  PMID: 8177741

Abstract

The type I DNA modification methylase M.EcoR124I binds sequence specifically to DNA and protects a 25bp fragment containing its cognate recognition sequence from digestion by exonuclease III. Using modified synthetic oligonucleotide duplexes we 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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