Structure at restriction endonuclease MboI cleavage sites protected by actinomycin D or distamycin A.
Restriction endonuclease MboI cleavage of DNA was inhibited by actinomycin D and distamycin A. The two inhibitors protected different subsets of the 8 cleavage sites in polyoma DNA. The cleavage reactions were analyzed both in the presence of minimal inhibitory concentrations of the compounds and at higher concentrations, allowing cleavage at only 1 site/DNA molecule. The experiments showed that cleavage sites most efficiently protected by actinomycin D had putative inhibitor binding sites at a distance of 1-2 base pairs from the MboI recognition sequence. Distamycin A, in contrast, apparently has to bind immediately adjacent to the MboI recognition sequence to protect from cleavage.
D001483:Base Sequence; D001665:Binding Sites; D004262:DNA Restriction Enzymes / Q000037:antagonists & inhibitors*; D004279:DNA, Viral; D003609:Dactinomycin / Q000494:pharmacology*; D015252:Deoxyribonucleases, Type II Site-Specific; D004214:Distamycins / Q000494:pharmacology*; D011120:Polyomavirus; D011758:Pyrroles / Q000494:pharmacology*
D004279:DNA, Viral; D004214:Distamycins; D011758:Pyrroles; D003609:Dactinomycin; C030000:stallimycin; D004262:DNA Restriction Enzymes; D015252:Deoxyribonucleases, Type II Site-Specific; C029312:GGTACC-specific type II deoxyribonucleases