Reverse gyrase recombination

This chapter describes the purification of reverse gyrases from their natural hosts and from recombinant Escherichia coli strains, in addition to the various assays developed to test their biochemical properties. Finally, the main structural features of these enzymes and their putative mechanism are discussed, together with their possible in vivo functions. 

Reverse gyrases have been purified from a number of organisms from both the Bacteria and Archaea Domains. More recently, recombinant versions have been... 

So far, the most successful expression of recombinant reverse gyrase has been from M kandleri, a unique type of reverse gyrase, made of two subunits. These... 

The unique enzymatic activity of reverses gyrases, i.e., the efficient production of positively supercoiled DNA, was used by a number of authors to estimate the impact of such a DNA structure on various biological mechanisms. These include chromatin stability,recombination, and transcription. However, the in vivo role of reverse gyrases in hyperthermophiles remains a matter of speculation. It was suggested long ago that one of the main functions of topoisomerases is to tightly... 

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