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

1989; Springer Nature; Volume: 8; Issue: 10 Linguagem: Inglês

10.1002/j.1460-2075.1989.tb08466.x

1460-2075

Christine Jaxel, Marc Nadal, Gilles Mirambeau, Patrick Forterre, Miho Takahashi, Michel Duguet,

Bioactive Compounds and Antitumor Agents

Research Article1 October 1989free access Reverse gyrase binding to DNA alters the double helix structure and produces single-strand cleavage in the absence of ATP. C. Jaxel C. Jaxel Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author M. Nadal M. Nadal Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author G. Mirambeau G. Mirambeau Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author P. Forterre P. Forterre Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author M. Takahashi M. Takahashi Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author M. Duguet M. Duguet Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author C. Jaxel C. Jaxel Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author M. Nadal M. Nadal Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author G. Mirambeau G. Mirambeau Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author P. Forterre P. Forterre Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author M. Takahashi M. Takahashi Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author M. Duguet M. Duguet Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. Search for more papers by this author Author Information C. Jaxel1, M. Nadal1, G. Mirambeau1, P. Forterre1, M. Takahashi1 and M. Duguet1 1Laboratoire d'Enzymologie des Acides Nucléiques, URA 3 CNRS, Université Pierre et Marie Curie, Paris, France. The EMBO Journal (1989)8:3135-3139https://doi.org/10.1002/j.1460-2075.1989.tb08466.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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, negatively supercoiled DNA was produced. This finding, obtained in the absence of ATP, contrasts with the ATP-dependent positive supercoiling catalyzed by reverse gyrase and is interpreted as the result of enzyme binding to DNA at high temperature. Another consequence of reverse gyrase stoichiometric binding to DNA is the formation of a cleavable complex which results in the production of single-strand breaks in the presence of detergent. Like eubacterial type I topoisomerase (protein omega), reverse gyrase is tightly attached to the 5′ termini of the cleaved DNA. In the light of these results, a comparison is tentatively made between reverse gyrase and the eubacterial type I (omega) and type II (gyrase) topoisomerases. Previous ArticleNext Article Volume 8Issue 101 October 1989In this issue RelatedDetailsLoading ...