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ID 14204
本文ファイル
著者
Tomita, Kazunori
Matsuura, Akira
Caspari, Thomas
Carr, Antony M.
Akamatsu, Yufuko
Iwasaki, Hiroshi
Mizuno, Ken-ichi
Ohta, Kunihiro
Uritani, Masahiro
Ushimaru, Takashi
Yoshinaga, Koichi
NDC
生物科学・一般生物学
抄録(英)
The Mre11-Rad50-Nbs1(Xrs2) complex and the Ku70-Ku80 heterodimer are thought to compete with each other for binding to DNA ends. To investigate the mechanism underlying this competition, we analyzed both DNA damage sensitivity and telomere overhangs in Schizosaccharomyces pombe rad50-d, rad50-d pku70-d, rad50-d exo1-d, and pku70-d rad50-d exo1-d cells. We found that rad50 exo1 double mutants are more methyl methanesulfonate (MMS) sensitive than the respective single mutants. The MMS sensitivity of rad50-d cells was suppressed by concomitant deletion of pku70+. However, the MMS sensitivity of the rad50 exo1 double mutant was not suppressed by the deletion of pku70+. The G-rich overhang at telomere ends in taz1-d cells disappeared upon deletion of rad50+, but the overhang reappeared following concomitant deletion of pku70+. Our data suggest that the Rad50 complex can process DSB ends and telomere ends in the presence of the Ku heterodimer. However, the Ku heterodimer inhibits processing of DSB ends and telomere ends by alternative nucleases in the absence of the Rad50-Rad32 protein complex. While we have identified Exo1 as the alternative nuclease targeting DNA break sites, the identity of the nuclease acting on the telomere ends remains elusive.
掲載誌名
Molecular and cellular biology
23巻
開始ページ
5186
終了ページ
5197
出版年月日
2003-08
出版者
American Society for Microbiology
ISSN
0270-7306
出版者DOI
PubMedID
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
Copyright (c) American Society for Microbiology
関連情報URL(IsVersionOf)
http://dx.doi.org/10.1128/MCB.23.15.5186-5197.2003
部局名
先端物質科学研究科