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Nucleic Acids Research, 1986, Vol. 14, No. 11 4543-4556
© 1986

Articles

Binding of the EcoRll methylase to azacytosine-containing DNA

Stanley Friedman

Department of Pharmacology, State University of New York, Downstate Medical Center Brooklyn, NY 11203, USA

Received February 12, 1986. Accepted May 8, 1986.

Binding of DNA(cytoaine-5)methyltransferases to azaoytosine containing DNA is stimulated by the presence of S-adenosyl-methionine or its analogs slnefungin or S-adenosyl-L-homo-cysteine. Methylation of the DNA is therefore not necessary for binding to occur. There Is no relationship between the affinity of the analog for the EooRII enzyme and its ability to Btinulate binding. The DNA-enzyme oomplex partially dissociates on incubation in 0.1% sodium dodeoyl sulfate and 0.5 H ammonium aoetate. Some of this DNA oould again form a tight complex with enzyme, indicating that DNA-enzyme oomplex formation is reversible. Binding occurs when the seoond oytosine in the sequence CCAGG is substituted by araoytoslne. This is the oytosine that would normally be methylated by the enzyme. The binding is therefore due to specific interaction of the methylase with azacyto-sine at the site it would normally methylate.


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