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

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

DNA topoisomerases signify a vital relations of DNA processing enzymes and a lot of topoisomerase inhibitors are used clinically for the remedy of assorted human cancers. Novels medications are in scientific improvement either opposed to style I and sort II topoisomerases. The e-book will comprise uncomplicated biochemical and structural studies for the cancer-relevant topoisomerases. it's going to describe how topoisomerase dysfunctions can harm the genome and raise the chance of cancers, and the involvement of topoisomerases in programmed telephone dying. The e-book also will current many of the topoisomerase inhibitors in medical use and improvement and their molecular and mobile mechanisms of action.

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The A. thaliana DNA gyrase subunits branch with those of cyanobacteria in phylogenetic analysis and can complement E. coli gyrase mutants (Forterre et al. 2007; Cho et al. 2004). Genetic analyses have shown that the DNA gyrase of A. thaliana is involved in the segregation of chloroplast DNA (Cho et al. 2004). Interestingly, DNA gyrase of A. thaliana is targeted to reach both chloroplasts and mitochondria (Wall et al. 2004). DNA gyrase genes are also present in the human malarial parasite Plasmodium falciparum and in other Plasmodium species (most likely via the chloroplastic route too, through secondary endosymbiois).

DNA gyrase genes are also present in the human malarial parasite Plasmodium falciparum and in other Plasmodium species (most likely via the chloroplastic route too, through secondary endosymbiois). The DNA gyrase of P. falciparum is indeed targeted exclusively to the apicoplast, an indispensable plasmid-like organelle, and is essential for apicoplast DNA replication (Dar et al. 2007; Raghu Ram et al. 2007). Beside Topo VI, already discussed, the DNA gyrase of Plasmodium should become another target for the search of new antimalarial drugs (Garcia-Estrada et al.

1995; Liu et al. 1995). This immediately suggested that Spo11 was this topoisomerase-like protein and, as a consequence, that Spo11 was responsible of chromosome cleavage during meiosis (Bergerat et al. 1997). This prediction was confirmed by site-directed mutagenesis of the yeast S. cerevisiae Spo11, guided by sequence comparison of the archaeal and yeast proteins. Replacement of the only tyrosine conserved between Spo11 and the A subunit of Topo VI by a phenylalanine turned out to inhibit the formation of meiotic-induced double-strand breaks in vivo (Bergerat et al.

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