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In the yeast, DSBs are repaired primarily by homologous recombination (HR). Since almost all HR events are significantly reduced in the <jats:italic>rad52<\/jats:italic> mutant cells, the Rad52 protein is believed to be a key component of HR in <jats:italic>S. cerevisiae<\/jats:italic>. Similarly to the <jats:italic>S. cerevisiae<\/jats:italic> Rad52 protein, RecA is the main HR protein in <jats:italic>Escherichia coli<\/jats:italic>. To address the question of whether the <jats:italic>E. coli<\/jats:italic> RecA protein can rescue HR defective phenotype of the <jats:italic>rad52<\/jats:italic> mutants of <jats:italic>S. cerevisiae<\/jats:italic>, the <jats:italic>recA<\/jats:italic> gene was introduced into the wild\u2010type and <jats:italic>rad52<\/jats:italic> mutant cells. Cell survival and DSBs induction and repair were studied in the RecA\u2010expressing wild\u2010type and <jats:italic>rad52<\/jats:italic> mutant cells after exposure to ionizing radiation (IR) and methyl methanesulphonate (MMS). Here, we show that expression of the <jats:italic>E. coli<\/jats:italic> RecA protein partially complemented sensitivity and fully complemented DSB repair defect of the <jats:italic>rad52<\/jats:italic> mutant cells after exposure to IR and MMS. We suggest that in the absence of Rad52, when all endogenous HR mechanisms are knocked out in <jats:italic>S. cerevisiae<\/jats:italic>, the heterologous <jats:italic>E. coli<\/jats:italic> RecA protein itself presumably takes over the broken DNA. 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