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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Detalhes bibliográficos
Publicado no:EMBO J
Main Authors: Jaxel, C, Nadal, M, Mirambeau, G, Forterre, P, Takahashi, M, Duguet, M
Formato: Artigo
Idioma:Inglês
Publicado em: Nature Publishing Group 1989
Assuntos:
Research Article
Acesso em linha: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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