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Structure at restriction endonuclease Mbo I cleavage sites protected by actinomycin D or distamycin A
Author(s) -
Nilsson Maj-Greth,
Skarped Catharina,
Magnusson Göran
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80200-7
Subject(s) - cleavage (geology) , dna , restriction enzyme , endonuclease , recognition sequence , biology , binding site , base pair , stereochemistry , restriction fragment , microbiology and biotechnology , chemistry , biochemistry , paleontology , fracture (geology)
Restriction endonuclease Mbo I 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 Mbo I recognition sequence. Distamycin A, in contrast, apparently has to bind immediately adjacent to the Mbo I recognition sequence to protect from cleavage.