Mouse Rad54 affects DNA conformation and DNA-damage-induced Rad51 foci formation

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Abstract

Error-free repair by homologous recombination of DNA double-strand breaks induced by ionizing radiation (IR) requires the Rad52 group proteins, including Rad51 and Rad54, in the yeast Saccharomyces cerevisiae [1]. The formation of a 'joint' molecule between the damaged DNA and the homologous repair template is a key step in recombination mediated by Rad51 and stimulated by Rad54 [2-5]. Mammalian homologs of Rad51 and Rad54 have been identified [2,3,6]. Here, we demonstrate that mouse Rad54 (mRad54) formed IR-induced nuclear foci that colocalized with mRad51. Interaction between mRad51 and mRad54 was induced by genotoxic stress, but only when lesions that required mRad54 for their repair were formed. Interestingly, mRad54 was essential for the formation of IR-induced mRad51 foci. Rad54 belongs to the SWI2/SNF2 protein family, members of which modulate protein-DNA interactions in an ATP-driven manner [7]. Results of a topological assay suggested that purified human Rad54 (hRad54) protein can unwind double-stranded (ds) DNA at the expense of ATP hydrolysis. Unwinding of the homologous repair template could promote the formation or stabilization of hRad51-mediated joint molecules. Rad54 appears to be required downstream of other Rad52 group proteins, such as Rad52 and the Rad55-Rad57 heterodimer, that assist Rad51 in interacting with the broken DNA [2-4].

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Tan, T. L. R., Essers, J., Citterio, E., Swagemakers, S. M. A., De Wit, J., Benson, F. E., … Kanaar, R. (1999). Mouse Rad54 affects DNA conformation and DNA-damage-induced Rad51 foci formation. Current Biology, 9(6), 325–328. https://doi.org/10.1016/S0960-9822(99)80142-0

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