DNA substrate specificity of reverse gyrase from extremely thermophilic archaebacteria.
It has been shown earlier that eukaryotic type I DNA topoisomerases act on duplex DNA regions, while eubacterial type I topoisomerases require single-stranded regions. The present paper demonstrates that the type I topoisomerase from extremely thermophilic archaebacteria, reverse gyrase, winds DNA by binding to single-stranded DNA regions. Thus, type I topoisomerases, both relaxing one in eubacteria and reverse gyrase in extremely thermophilic archaebacteria share a substrate specificity to melted DNA regions. The important consequence of this specificity is that the cellular DNA superhelical stress actively controlled by bacterial topoisomerases is confined to a narrow range characterized by a low stability of the double helix. Hence we suppose that bacterial topoisomerase systems control duplex stability near its minimum, for which purpose they create an appropriate negative superhelicity at moderate temperatures or a positive one at extremely high temperatures, the feedback being ensured by the aforesaid specificity of type I bacterial topoisomerases.
Slesarev
A I
AI
Institute of Molecular Genetics, USSR Academy of Sciences, Moscow.
Kozyavkin
S A
SA
D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D004264:DNA Topoisomerases, Type I; D004250:DNA Topoisomerases, Type II / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism / Q000494:pharmacology; D006358:Hot Temperature; D009691:Nucleic Acid Denaturation; D013379:Substrate Specificity; D059005:Topoisomerase II Inhibitors
D004277:DNA, Single-Stranded; D059005:Topoisomerase II Inhibitors; C041813:DNA reverse gyrase; D004264:DNA Topoisomerases, Type I; D004250:DNA Topoisomerases, Type II