CHARACTERIZATION OF A REVERSE GYRASE FROM THE EXTREMELY THERMOPHILIC HYDROGEN-OXIDIZING EUBACTERIUM CALDEROBACTERIUM-HYDROGENOPHILUM

被引：15

作者：

ANDERA, L

MIKULIK, K

SAVELYEVA, ND

机构：

[1] CZECHOSLOVAK ACAD SCI, INST MICROBIOL, CS-11142 PRAGUE 1, CZECHOSLOVAKIA

[2] ACAD SCI RUSSIAN REPUBL, INST MICROBIOL, MOSCOW, RUSSIA

来源：

FEMS MICROBIOLOGY LETTERS | 1993年 / 110卷 / 01期

关键词：

REVERSE GYRASE; EUBACTERIUM; CALDEROBACTERIUM-HYDROGENOPHILUM; DNA SUPERCOILING;

D O I：

10.1111/j.1574-6968.1993.tb06303.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Reverse gyrase was isolated from an extremely thermophilic hydrogen-oxidizing eubacterium Calderobacterium hydrogenophilum. The enzyme catalyses the introduction of positive supercoils into the covalent closed DNA and requires ATP or dATP for its activity. So far, reverse gyrase has been purified to homogeneity only from thermophilic archaebacteria. Reverse gyrase from C. hydrogenophilum such as the archaebacterial enzymes is a monomeric protein and has a molecular mass between 115 and 120 kDa. The optimal reaction temperature is 90-degrees-C and the thermostability of this reverse gyrase is remarkable. The enzyme retains more than 95% of the activity after 40 min of incubation at 100-degrees-C.

引用

页码：107 / 112

页数：6

共 22 条

[1]

ANDERA L, 1991, BIOCHEM BIOPH RES CO, V175, P949

[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] DISTRIBUTION OF REVERSE GYRASE IN REPRESENTATIVE SPECIES OF EUBACTERIA AND ARCHAEBACTERIA [J].