Mirambeau G, Duguet M, Forterre P
J Mol Biol. 1984 Nov 5;179(3):559-63. doi: 10.1016/0022-2836(84)90080-9.
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.
一种能够使负超螺旋DNA松弛的拓扑异构酶已从古细菌嗜酸热硫化叶菌中分离出来。在70摄氏度至80摄氏度之间，体外松弛反应完全有效，且依赖于ATP和镁离子的存在。该酶不表现出类似促旋酶的活性，对促旋酶抑制剂的敏感性也很低。这些特性让人联想到真核生物II型拓扑异构酶。然而，该酶无法使正超螺旋DNA松弛。这种嗜热酶可用于多种方式来研究高温下DNA的结构和稳定性。
