Natassja G Bush, Katherine Evans-Roberts, Anthony Maxwell
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DNA topoisomerases are enzymes that control the topology of DNA in all cells. There are two types, I and II, classified according to whether they make transient single- or double-stranded breaks in DNA. Their reactions generally involve the passage of a single- or double-strand segment of DNA through this transient break, stabilized by DNA-protein covalent bonds. All topoisomerases can relax DNA, but DNA gyrase, present in all bacteria, can also introduce supercoils into DNA. Because of their essentiality in all cells and the fact that their reactions proceed via DNA breaks, topoisomerases have become important drug targets; the bacterial enzymes are key targets for antibacterial agents. This article discusses the structure and mechanism of topoisomerases and their roles in the bacterial cell. Targeting of the bacterial topoisomerases by inhibitors, including antibiotics in clinical use, is also discussed.
EcoSal PlusImmunology and Microbiology-Microbiology
CiteScore
12.20
自引率
0.00%
发文量
4
期刊介绍:
EcoSal Plus is the authoritative online review journal that publishes an ever-growing body of expert reviews covering virtually all aspects of E. coli, Salmonella, and other members of the family Enterobacteriaceae and their use as model microbes for biological explorations. This journal is intended primarily for the research community as a comprehensive and continuously updated archive of the entire corpus of knowledge about the enteric bacterial cell. Thoughtful reviews focus on physiology, metabolism, genetics, pathogenesis, ecology, genomics, systems biology, and history E. coli and its relatives. These provide the integrated background needed for most microbiology investigations and are essential reading for research scientists. Articles contain links to E. coli K12 genes on the EcoCyc database site and are available as downloadable PDF files. Images and tables are downloadable to PowerPoint files.