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pubmed-article:1315962pubmed:abstractTextA guanine-rich single-stranded DNA from the human immunoglobulin switch region was shown by Sen and Gilbert [Nature, (1988) 334, 364-366] to be able to self-associate to form a stable four-stranded parallel DNA structure. Topoisomerase II did not cleave the single-stranded DNA molecule. Surprisingly, the enzyme did cleave the same DNA sequence when it was annealed into the four-stranded structure. The two cleavage sites observed were the same as those found when this DNA molecule was paired with a complementary molecule to create a normal B-DNA duplex. These cleavages were shown to be protein-linked and reversible by the addition of salt, suggesting a normal topoisomerase II reaction mechanism. In addition, an eight-stranded DNA molecule created by the association of a complementary oligonucleotide with the four-stranded structure was also cleaved by topoisomerase II despite being resistant to restriction endonuclease digestion. These results suggest that a single strand of DNA may possess the sequence information to direct topoisomerase II to a binding site, but the site must be base paired in a proper manner to do so. This demonstration of the ability of a four-stranded DNA molecule to be a substrate for an enzyme further suggests that these DNA structures may be present in cells.lld:pubmed
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pubmed-article:1315962pubmed:articleTitleEukaryotic topoisomerase II cleavage of parallel stranded DNA tetraplexes.lld:pubmed
pubmed-article:1315962pubmed:affiliationDepartment of Molecular Genetics, Ohio State University, Columbus 43210.lld:pubmed
pubmed-article:1315962pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1315962pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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