Reverse gyrase binding to DNA alters the double helix structure and produces single-strand cleavage in the absence of ATP.

Stoichiometric amounts of pure reverse gyrase, a type I topoisomerase from the archaebacterium Sulfolobus acidocaldarius were incubated at 75 degrees C with circular DNA containing a single-chain scission. After covalent closure by a thermophilic ligase and removal of bound protein molecules, negati...

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Vydáno v:	EMBO J
Hlavní autoři:	Jaxel, C, Nadal, M, Mirambeau, G, Forterre, P, Takahashi, M, Duguet, M
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Nature Publishing Group 1989
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC401394/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2555155/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1989.tb08466.x
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