An atypical topoisomerase II from archaea with implications for meiotic recombination

Agnès Bergerat, Bernard de Massy, Danielle Gadelle, Paul-Christophe Varoutas, Alain Nicolas and Patrick Forterre
Additional contact information
Agnès Bergerat: Université Paris Sud
Bernard de Massy: Section de Recherche
Danielle Gadelle: Université Paris Sud
Paul-Christophe Varoutas: Section de Recherche
Alain Nicolas: Section de Recherche
Patrick Forterre: Université Paris Sud

Nature, 1997, vol. 386, issue 6623, 414-417

Abstract: Abstract Type II topoisomerases help regulate DNA topology during transcription, replication and recombination by catalysing DNA strand transfer through transient double-stranded breaks1. All type II topoisomerases described so far are members of a single protein family2. We have cloned and sequenced the genes encoding the A and B subunits of topoisomerase II from the archaeon Sulfolobus shibatae. This enzyme is the first of a new family. It has no similarity with other type II topoisomerases, except for three motifs in the B subunit probably involved in ATP binding and hydrolysis. We also found these motifs in proteins of the Hsp903 and MutL4 families. The A subunit has similarities with four proteins of unknown function. One of them, the Saccharomyces cerevisiae Spo115 protein, is required for the initiation of meiotic recombination. Mutagenesis, performed on SPO11, of the single tyrosine conserved between the five homologues shows that this amino acid is essential for Spo11 activity. By analogy with the mechanism of action of known type II topoisomerases, we suggest that Spo11 catalyses the formation of double-strand breaks that initiate meiotic recombination in S. cerevisiae.

Date: 1997
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DOI: 10.1038/386414a0

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