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http://purl.uniprot.org/citations/3038879http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3038879http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3038879http://www.w3.org/2000/01/rdf-schema#comment"Reverse gyrase is a type I DNA topoisomerase that promotes positive supercoiling of closed-circular double-stranded DNA through an ATP-dependent reaction, and it was purified from an archaebacterium, Sulfolobus. When ATP is replaced by UTP, GTP, or CTP, this enzyme just relaxes the negatively supercoiled closed-circular double-stranded DNA. We found that reverse gyrase hydrolyzes ATP through a double-stranded DNA-dependent reaction. The superhelicity of the DNA did not affect the ATPase activity. However, reverse gyrase does not hydrolyze UTP, GTP, or CTP. Therefore, any of the four nucleotide 5'-triphosphates acts as an effector for the topoisomerase activity of reverse gyrase, but only ATP supports the positive supercoiling of closed-circular double-stranded DNA, through the energy released on its hydrolysis. Single-stranded DNA was a much more potent cofactor for the ATPase activity of the enzyme than double-stranded DNA, and it acted as a potent inhibitor for the topoisomerase activity on double-stranded DNA. These results indicate that reverse gyrase has higher affinity to single-stranded DNA than to double-stranded DNA, which suggests a cellular function of the enzyme."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)60974-3"xsd:string
http://purl.uniprot.org/citations/3038879http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)60974-3"xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Shibata T."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Shibata T."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Nakasu S."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Nakasu S."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Yasui K."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/author"Yasui K."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/pages"10419-10421"xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/pages"10419-10421"xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/title"Intrinsic DNA-dependent ATPase activity of reverse gyrase."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/title"Intrinsic DNA-dependent ATPase activity of reverse gyrase."xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/volume"262"xsd:string
http://purl.uniprot.org/citations/3038879http://purl.uniprot.org/core/volume"262"xsd:string
http://purl.uniprot.org/citations/3038879http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3038879
http://purl.uniprot.org/citations/3038879http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3038879