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タイトル
和文:A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity. 
英文:A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity 
著者
和文: 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.  
英文: 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.  
言語 English 
掲載誌/書名
和文: 
英文:Proceedings of the National Academy of Sciences of the United States of America 
巻, 号, ページ Vol. 118    No. 11    e2016287118
出版年月 2021年3月16日 
出版者
和文: 
英文:National Academy of Sciences 
会議名称
和文: 
英文: 
開催地
和文: 
英文: 
公式リンク http://europepmc.org/abstract/med/33836577
 
DOI https://doi.org/10.1073/pnas.2016287118
アブストラクト 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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