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Nucleic Acids Research, Vol 26, Issue 7 1668-1674, Copyright © 1998 by Oxford University Press

ARTICLES

Sequence specific interaction of Mycobacterium smegmatis topoisomerase I with duplex DNA

T Bhaduri, D Sikder and V Nagaraja
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.

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.
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D. Sikder and V. Nagaraja
Determination of the recognition sequence of Mycobacterium smegmatis topoisomerase I on mycobacterial genomic sequences
Nucleic Acids Res., April 15, 2000; 28(8): 1830 - 1837.
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