DNA Topoisomerases and Cancer by Patrick Forterre (auth.), Yves Pommier (eds.)

By Patrick Forterre (auth.), Yves Pommier (eds.)

DNA topoisomerases characterize an important relations of DNA processing enzymes and plenty of topoisomerase inhibitors are used clinically for the remedy of varied human cancers. Novels medicines are in scientific improvement either opposed to sort I and kind II topoisomerases. The e-book will comprise easy biochemical and structural stories for the cancer-relevant topoisomerases. it's going to describe how topoisomerase dysfunctions can harm the genome and bring up the chance of cancers, and the involvement of topoisomerases in programmed mobile loss of life. The e-book also will current many of the topoisomerase inhibitors in scientific use and improvement and their molecular and mobile mechanisms of action.

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Structural analyses allowed defining more clearly their evolutionary relationships. The lack of similarity between the Topo IIA and Topo IB A subunits was confirmed by the resolution of the structure of the A subunit of the M. jannashii Topo VI (Nichols et al. 1999). Although all Topo II contain similar folds, such as Toprim domain (also present in Topo IA), and CAP-like domains, these folds are organized in different orders and the overall structure of the two proteins is not similar. The B subunits of Topo IIA and Topo IIB are homologous, as deduced from their structural comparison, although they share only limited sequence similarities (Corbett and Berger 2003).

2007). Finally, the discovery of Topo IIB has dramatically exemplified the importance to take into account the diversity of the living world to mine for new forms of already well-known enzymatic activity. For a long time, such search has been mainly driven by the curiosity of a few scientists and success was dependent on both luck and the choice of the good organism. After the genomic revolution, our search for new enzymes can be guided by in silico data and, as a consequence, the search for new model systems could be rationalized.

1 Introduction and Historical Perspective 17 nevertheless remaining strongly bond to the Topo I during that reaction (Koster et al. 2005)). Although Topo I are often defined as enzymes that change the Lk by step of 1, the controlled rotation mechanism catalyzed by Topo IB can actually changes the Lk by more than one during a single cleavage/religation cycle (Fig. 4). 2 Topo IIA Are Diverse but Homologous In contrast to Topo I, sequence analyses revealed that all Topo II known in the eighties belong to a same protein family (Fig.

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