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Title
Japanese:A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity. 
English:A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity 
Author
Japanese: Aleksandar Zdravković, James M. Daley, Arijit Dutta, Tatsuya Niwa, Yasuto Murayama, Shuji Kanamaru, Kentaro Ito, Takahisa Maki, Bilge Argunhan, Masayuki Takahashi, Hideo Tsubouchi, Patrick Sung, Hiroshi Iwasaki.  
English: Aleksandar Zdravković, James M. Daley, Arijit Dutta, Tatsuya Niwa, Yasuto Murayama, Shuji Kanamaru, Kentaro Ito, Takahisa Maki, Bilge Argunhan, Masayuki Takahashi, Hideo Tsubouchi, Patrick Sung, Hiroshi Iwasaki.  
Language English 
Journal/Book name
Japanese: 
English:Proceedings of the National Academy of Sciences of the United States of America 
Volume, Number, Page Vol. 118    No. 11    e2016287118
Published date Mar. 16, 2021 
Publisher
Japanese: 
English:National Academy of Sciences 
Conference name
Japanese: 
English: 
Conference site
Japanese: 
English: 
File
Official URL http://europepmc.org/abstract/med/33836577
 
DOI https://doi.org/10.1073/pnas.2016287118
Abstract A DNA double-strand break (DSB) can be repaired accurately by homologous recombination. The Mre11-Rad50-Nbs1 (MRN) complex is responsible for initiating homologous recombination by degrading 5′-ended DNA strand, where its activation by the Ctp1 cofactor plays a pivotal role. Here, by using purified fission yeast proteins, we show that two major elements comprise MRN activation. First, phosphorylation of Ctp1 promotes the physical interaction between MRN and Ctp1. Second, the C terminus of Ctp1 activates nucleolytic processing of DSB ends. In the latter case, a small peptide comprising only 15 amino acids from the Ctp1 C terminus is sufficient to activate MRN. Our results elucidate the core elements underlying MRN activation by Ctp1.

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