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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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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
1989
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC401394/ https://ncbi.nlm.nih.gov/pubmed/2555155 |
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