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Comparative Study
. 1987 Aug 25;909(3):201-7.
doi: 10.1016/0167-4781(87)90078-9.

Interaction of AluI, Cfr6I and PvuII restriction-modification enzymes with substrates containing either N4-methylcytosine or 5-methylcytosine

V Butkus, S Klimasauskas, L Petrauskiene, Z Maneliene, A Lebionka, A Janulaitis
Comparative Study

Interaction of AluI, Cfr6I and PvuII restriction-modification enzymes with substrates containing either N4-methylcytosine or 5-methylcytosine

V Butkus et al. Biochim Biophys Acta. .

Abstract

The cleavage specificity of R.Cfr6I, an isoschizomer of PvuII restriction endonuclease was determined to be 5'CAG decreases CTG and the methylation specificity of Cfr6I and PvuII methylases, 5'CAG4mCTG. Thus, M.Cfr6I and M.PvuII are new additions to the list of methylases with N4-methylcytosine specificity. Neither of the above RM enzymes acts on the substrates containing either N4-methylcytosine or 5-methylcytosine in a cognate methylation position.

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