http://purl.uniprot.org/citations/3038879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3038879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3038879 | http://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/3038879 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)60974-3"xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)60974-3"xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Shibata T."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Shibata T."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Kikuchi A."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Kikuchi A."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Nakasu S."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Nakasu S."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Yasui K."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/author | "Yasui K."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/pages | "10419-10421"xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/pages | "10419-10421"xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/title | "Intrinsic DNA-dependent ATPase activity of reverse gyrase."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/title | "Intrinsic DNA-dependent ATPase activity of reverse gyrase."xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/volume | "262"xsd:string |
http://purl.uniprot.org/citations/3038879 | http://purl.uniprot.org/core/volume | "262"xsd:string |
http://purl.uniprot.org/citations/3038879 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3038879 |
http://purl.uniprot.org/citations/3038879 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3038879 |