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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Detaylı Bibliyografya
Asıl Yazarlar: Jaxel, C, Nadal, M, Mirambeau, G, Forterre, P, Takahashi, M, Duguet, M
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1989
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC401394/
https://ncbi.nlm.nih.gov/pubmed/2555155
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