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The In Vitro Characterization of the Role of Rad57 in Rad51 Catalyzed Homologous Recombination Repair

The homologous recombination of DNA is necessary for the accurate repair of double‐strand DNA breaks. The activity of this repair pathway must remain at an appropriate level; repair must effectively recover stalled or broken replication forks, without leading to genomic instability and cancer. This balance requires precise control over these reactions. A number of proteins involved in DNA repair mechanisms have been identified; some have been studied extensively, and their functions and biochemical roles characterized. Other proteins have yet to be studied, and their role in recombination remains unclear. The Rad57 protein has been identified as a RA51 paralog and is thought to play a role in regulating Rad51 activities in homologous recombination. However, to date few studies have focused on specifically analyzing the biochemical functions of Rad57. To better understand the functions of Rad57 in homologous recombination, we have cloned, expressed, purified Rad57 and characterized its biochemical activities surrounding homologous recombination. The characterized activities of Rad57 include its DNA binding properties and its effect on Rad51 catalyzed actions.