Open AccessCharacterization of a reverse gyrase from the extremely thermophilic hydrogen‐oxidizing eubacterium Calderobacterium hydrogenophilum
Author(s) -
Andera Ladislav,
Mikulik Karel,
Savelyeva Nadja D.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06303.x
Subject(s) - thermophile , eubacterium , thermostability , dna gyrase , biochemistry , dna supercoil , enzyme , biology , chemistry , escherichia coli , microbiology and biotechnology , bacteria , dna , genetics , dna replication , gene
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°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°C.