TY - JOUR TI - Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex AU - Argunhan, Bilge AU - Sakakura, Masayoshi AU - Afshar, Negar AU - Kurihara, Misato AU - Ito, Kentaro AU - Maki, Takahisa AU - Kanamaru, Shuji AU - Murayama, Yasuto AU - Tsubouchi, Hideo AU - Takahashi, Masayuki AU - Takahashi, Hideo AU - Iwasaki, Hiroshi A2 - Heyer, Wolf-Dietrich A2 - Wolberger, Cynthia A2 - Heyer, Wolf-Dietrich VL - 9 PY - 2020 DA - 2020/03/24 SP - e52566 C1 - eLife 2020;9:e52566 DO - 10.7554/eLife.52566 UR - https://doi.org/10.7554/eLife.52566 AB - Although Rad51 is the key protein in homologous recombination (HR), a major DNA double-strand break repair pathway, several auxiliary factors interact with Rad51 to promote productive HR. We present an interdisciplinary characterization of the interaction between Rad51 and Swi5-Sfr1, a conserved auxiliary factor. Two distinct sites within the intrinsically disordered N-terminus of Sfr1 (Sfr1N) were found to cooperatively bind Rad51. Deletion of this domain impaired Rad51 stimulation in vitro and rendered cells sensitive to DNA damage. By contrast, amino acid-substitution mutants, which had comparable biochemical defects, could promote DNA repair, suggesting that Sfr1N has another role in addition to Rad51 binding. Unexpectedly, the DNA repair observed in these mutants was dependent on Rad55-Rad57, another auxiliary factor complex hitherto thought to function independently of Swi5-Sfr1. When combined with the finding that they form a higher-order complex, our results imply that Swi5-Sfr1 and Rad55-Rad57 can collaboratively stimulate Rad51 in Schizosaccharomyces pombe. KW - DNA repair KW - homologous recombination KW - Rad51 KW - Swi5-Sfr1 KW - Rad55-Rad57 KW - disordered JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -