DNA gyrase from Escherichia coli has been used in a study to investigate a comparative proteomic approach to better define Deinococcus nucleoid specificities. DNA gyrase from Escherichia coli has also been used in a study to investigate the role of the DnaK-ClpB bichaperone system in DNA gyrase reactivation.
DNA gyrase is supplied as an A2B2 holoenzyme. The molecular mass of subunit A is 97 kDa and that of subunit B is 90 kDa. It catalyzes the ATP-dependent introduction of negative supercoils into relaxed DNA. DNA gyrase has been successfully converted into a type II topoisomerase by mutagenesis experiments.
