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- W2151729897 abstract "We have identified strong topoisomerase sites (STS) for Mycobacteruim smegmatis topoisomerase I in double-stranded DNA context using electrophoretic mobility shift assay of enzyme-DNA covalent complexes. Mg2+, an essential component for DNA relaxation activity of the enzyme, is not required for binding to DNA. The enzyme makes single-stranded nicks, with transient covalent interaction at the 5'-end of the broken DNA strand, a characteristic akin to prokaryotic topoisomerases. More importantly, the enzyme binds to duplex DNA having a preferred site with high affinity, a property similar to the eukaryotic type I topoisomerases. The preferred cleavage site is mapped on a 65 bp duplex DNA and found to be CG/TCTT. Thus, the enzyme resembles other prokaryotic type I topoisomerases in mechanistics of the reaction, but is similar to eukaryotic enzymes in DNA recognition properties." @default.
- W2151729897 created "2016-06-24" @default.
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- W2151729897 date "1998-04-01" @default.
- W2151729897 modified "2023-09-26" @default.
- W2151729897 title "Sequence specific interaction of Mycobacterium smegmatis topoisomerase I with duplex DNA" @default.
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- W2151729897 doi "https://doi.org/10.1093/nar/26.7.1668" @default.
- W2151729897 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/147473" @default.
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