Phylogenomics of type II DNA topoisomerases

@article{Gadelle2003PhylogenomicsOT,
  title={Phylogenomics of type II DNA topoisomerases},
  author={Daniele Gadelle and Jonathan Fil{\'e}e and Cyril Buhler and Patrick Forterre},
  journal={BioEssays},
  year={2003},
  volume={25}
}
Type II DNA topoisomerases (Topo II) are essential enzymes implicated in key nuclear processes. The recent discovery of a novel kind of Topo II (DNA topoisomerase VI) in Archaea led to a division of these enzymes into two non‐homologous families, (Topo IIA and Topo IIB) and to the identification of the eukaryotic protein that initiates meiotic recombination, Spo11. In the present report, we have updated the distribution of all Topo II in the three domains of life by a phylogenomic approach… 

Viral origin of eukaryotic type IIA DNA topoisomerases

The topology of the tree suggests that the eukaryotic Topo IIA was probably acquired from an ancestral member of the Nucleocytoviricota of the class Megaviricetes, before the emergence of the last eUKaryotic common ancestor (LECA).

DNA topoisomerase VIII: a novel subfamily of type IIB topoisomerases encoded by free or integrated plasmids in Archaea and Bacteria

Bacterial genes encoding a topoisomerase VIII, the smallest known type IIB enzymes, could be new promising models for structural and mechanistic studies.

Topoisomerases of kinetoplastid parasites: why so fascinating?

This review summarizes the recent advances in research in kinetoplastid topoisomerases, their evolutionary significance and the death of the unicellular parasite Leishmania donovani induced by topoisomersase I inhibitor camptothecin.

A DNA topoisomerase IB in Thaumarchaeota testifies for the presence of this enzyme in the last common ancestor of Archaea and Eucarya

It is shown that a eukaryotic-like TopoIB is present in the recently sequenced genomes of two archaea of the newly proposed phylum Thaumarchaeota, indicating that the last common ancestor of Archaea and Eucarya may have harboured a DNA genome.

Evolutionary History of TOPIIA Topoisomerases in Animals

It is shown that TOPIIA is highly conserved in Metazoa, and two amino acid substitutions are found suggesting that TOP2A may have contributed to the evolution of present-day humans, as proposed for other cell cycle-related genes.

Phylogenomics of DNA topoisomerases: their origin and putative roles in the emergence of modern organisms

It is proposed that topoisomerases originated in an ancestral virosphere, and that various subfamilies were later on transferred independently to different ancient cellular lineages, and played a critical role in the origin of modern genomes and in the emergence of the three cellular domains.

Inhibition of archaeal growth and DNA topoisomerase VI activities by the Hsp90 inhibitor radicicol

It is found that radicicol can theoretically fit in the ATP-binding pocket of the DNA topoisomerase VI ‘Bergerat fold’, whereas geldanamycin cannot.

DNA Topoisomerases of Kinetoplastid Parasites: Brief Overview and Recent Perspectives.

Historical perspectives and recent advances in kinetoplastid topoisomerase research are summarized and how these proteins are exploited for drug targeting are summarized.
...

References

SHOWING 1-10 OF 61 REFERENCES

An atypical topoisomerase II from archaea with implications for meiotic recombination

It is suggested that Spo11 catalyses the formation of double-strand breaks that initiate meiotic recombination in S. cerevisiae by analogy with the mechanism of action of known type II topoisomerases.

Topoisomerase II from Chlorella Virus PBCV-1

The PBCV-1 enzyme is considerably smaller than other eukaryotic topoisomerase II enzymes (whose molecular masses are typically 160–180 kDa), it displays all the catalytic properties expected for a type II topoisomersase.

DNA topoisomerases: structure, function, and mechanism.

Surprisingly, despite little or no sequence homology, both type IA and type IIA topoisomerases from prokaryotes and the typeIIA enzymes from eukaryotes share structural folds that appear to reflect functional motifs within critical regions of the enzymes.

Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11

The A subunit of topoisomerase VI is homologous to the meiotic recombination factor, Spo11, and this structure can serve as a template for probing Spo11 function in eukaryotes.

Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins.

The common ancestor of all life forms could encode a prototype Toprim enzyme that might have had both nucleotidyl transferase and polynucleotide cleaving activity, supported by site-directed mutagenesis data on primases and Topo IA.

Eukaryotic DNA topoisomerase II beta.

  • C. AustinK. Marsh
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1998
The research on DNA topoisomerase II beta over the last 10 years is reviewed, finding the role of the beta isoform is not yet clear.

Investigating the biological functions of DNA topoisomerases in eukaryotic cells.

  • J. Nitiss
  • Biology
    Biochimica et biophysica acta
  • 1998

Conversion of DNA gyrase into a conventional type II topoisomerase.

  • S. KampranisA. Maxwell
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1996
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.
...