| pubmed-article:8962066 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8962066 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:8962066 | lifeskim:mentions | umls-concept:C0949782 | lld:lifeskim |
| pubmed-article:8962066 | lifeskim:mentions | umls-concept:C1336767 | lld:lifeskim |
| pubmed-article:8962066 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:8962066 | lifeskim:mentions | umls-concept:C0439858 | lld:lifeskim |
| pubmed-article:8962066 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:8962066 | pubmed:dateCreated | 1997-1-15 | lld:pubmed |
| pubmed-article:8962066 | pubmed:abstractText | DNA gyrase is unique among topoisomerases in its ability to introduce negative supercoils into closed-circular DNA. We have demonstrated that deletion of the C-terminal DNA-binding domain of the A subunit of gyrase gives rise to an enzyme that cannot supercoil DNA but relaxes DNA in an ATP-dependent manner. Novobiocin, a competitive inhibitor of ATP binding by gyrase, inhibits this reaction. The truncated enzyme, unlike gyrase, does not introduce a right-handed wrap when bound to DNA and stabilizes DNA crossovers; characteristics reminiscent of conventional type II topoisomerases. This new enzyme form can decatenate DNA circles with increased efficiency compared with intact gyrase and, as a result, can complement the temperature-sensitive phenotype of a parCts mutant. Thus these results suggest that the unique properties of DNA gyrase are attributable to the wrapping of DNA around the C-terminal DNA-binding domains of the A subunits and provide an insight into the mechanism of type II topoisomerases. | lld:pubmed |
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| pubmed-article:8962066 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8962066 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8962066 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8962066 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8962066 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8962066 | pubmed:author | pubmed-author:MaxwellAA | lld:pubmed |
| pubmed-article:8962066 | pubmed:author | pubmed-author:KampranisS... | lld:pubmed |
| pubmed-article:8962066 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8962066 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:8962066 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8962066 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8962066 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8962066 | pubmed:pagination | 14416-21 | lld:pubmed |
| pubmed-article:8962066 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8962066 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8962066 | pubmed:articleTitle | Conversion of DNA gyrase into a conventional type II topoisomerase. | lld:pubmed |
| pubmed-article:8962066 | pubmed:affiliation | Department of Biochemistry, University of Leicester, United Kingdom. | lld:pubmed |
| pubmed-article:8962066 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8962066 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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