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. 2004 Jun 10;32(10):3148–3155. doi: 10.1093/nar/gkh638

Figure 5.

Figure 5

Figure 5

Phosphate contacts of KpnI REase (A) and MTase (B) upon binding to their recognition sequence as revealed by ethylation interference analysis. The labeled (top or bottom strand) duplex oligonucleotides were modified by addition of saturated ethylnitrosourea. The modified DNA was incubated with KpnI REase (200 nM) and MTase (250 mM). The free and bound fractions were separated by 8% native PAGE and purified. The cleavage products were analyzed by 15% PAGE as described. The modified phosphates within the recognition sequence, which interfere with REase binding to DNA, are indicated. Similarly, modified phosphates, which favored MTase binding, are shown. Lane G = the G ladder; lane F = free DNA; lane C = bound DNA.