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Title
Japanese: 
English:Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex 
Author
Japanese: アルグンハンビルゲ, 坂倉正義, AfsharNegar, Kurihara, M., 伊藤健太郎, 真木孝尚, 金丸周司, 村山泰斗, 坪内英生, Masayuki Takahashi, 高橋栄夫, 岩崎博史.  
English: Argunhan Bilge, Masayoshi Sakakura, Negar Afshar, Kurihara, M., Kentarou Itou, Takahisa Maki, Shuji Kanamaru, Yasuto Murayama, Hideo Tsubouchi, Masayuki Takahashi, Hideo Takahashi, Hiroshi Iwasaki.  
Language English 
Journal/Book name
Japanese:eLife 
English:eLife 
Volume, Number, Page Vol. 9    No. e52566   
Published date Mar. 2020 
Publisher
Japanese: 
English:eLife Sciences Publications 
Conference name
Japanese: 
English: 
Conference site
Japanese: 
English: 
File
Official URL http://www.scopus.com/inward/record.url?eid=2-s2.0-85082260964&partnerID=MN8TOARS
 
DOI https://doi.org/10.7554/eLife.52566
Abstract 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.

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