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An atypical topoisomerase II from Archaea with implications for meiotic recombination

机译：来自古细菌的非典型拓扑异构酶II，对减数分裂重组有影响

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摘要

Type II topoisomerases help regulate DNA topology during transcription, replication and recombination by catalysing DNA strand transfer through transient double-stranded breaks. All type II topoisomerases described so far are members of a single protein family. 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 Hsp90 and MutL families. The A subunit has similarities with four proteins of unknown function. One of them, the Saccharomyces cerevisiae Spo11 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.
机译：II型拓扑异构酶可通过短暂的双链断裂催化DNA链转移，从而在转录，复制和重组过程中帮助调节DNA拓扑结构。到目前为止描述的所有II型拓扑异构酶都是单个蛋白质家族的成员。我们已经克隆和测序了古细菌Sulfolobus shibatae的拓扑异构酶II的A和B亚基的编码基因。这种酶是新家族的第一个。它与其他II型拓扑异构酶没有相似之处，只是B亚基中的三个基序可能与ATP结合和水解有关。我们还在Hsp90和MutL家族的蛋白质中发现了这些基序。 A亚基与四种功能未知的蛋白质具有相似性。其中之一，酿酒酵母Spo11蛋白，是减数分裂重组启动所必需的。对五个同系物之间保守的单个酪氨酸进行SPO11诱变，表明该氨基酸对Spo11活性至关重要。通过类推与已知的II型拓扑异构酶的作用机理，我们建议Spo11催化双链断裂的形成，从而引发酿酒酵母中的减数分裂重组。

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