ATP-dependent DNA topoisomerase from the archaebacterium Sulfolobus acidocaldarius. Relaxation of supercoiled DNA at high temperature.
A topoisomerase, able to relax negatively supercoiled DNA, has been isolated from the archaebacterium Sulfolobus acidocaldarius. Relaxation was fully efficient in vitro between 70 degrees C and 80 degrees C and was dependent on the presence of ATP and magnesium ions. The enzyme did not exhibit gyrase-like activity and was poorly sensitive to gyrase inhibitors. These properties are reminiscent of eukaryotic type II topoisomerases. However, the enzyme was unable to relax positively supercoiled DNA. This thermophilic enzyme may be used in a variety of ways to study the structure and stability of DNA at high temperature.
D000255:Adenosine Triphosphate; D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D004264:DNA Topoisomerases, Type I / Q000302:isolation & purification; D004269:DNA, Bacterial; D004278:DNA, Superhelical; D004587:Electrophoresis, Agar Gel; D007700:Kinetics; D008274:Magnesium; D009690:Nucleic Acid Conformation; D013696:Temperature
D004269:DNA, Bacterial; D004278:DNA, Superhelical; D000255:Adenosine Triphosphate; D004264:DNA Topoisomerases, Type I; D008274:Magnesium