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Title: Accumulation of Ku70 at DNA double-strand breaks in living epithelial cells

Abstract

Ku70 and Ku80 play an essential role in the DNA double-strand break (DSB) repair pathway, i.e., nonhomologous DNA-end-joining (NHEJ). No accumulation mechanisms of Ku70 at DSBs have been clarified in detail, although the accumulation mechanism of Ku70 at DSBs plays key roles in regulating the NHEJ activity. Here, we show the essential domains for the accumulation and function of Ku70 at DSBs in living lung epithelial cells. Our results showed that EGFP-Ku70 accumulation at DSBs began immediately after irradiation. Our findings demonstrate that three domains of Ku70, i.e., the {alpha}/{beta}, DNA-binding, and Ku80-binding domains, but not the SAP domain, are necessary for the accumulation at or recognition of DSBs in the early stage after irradiation. Moreover, our findings demonstrate that the leucine at amino acid 385 of Ku70 in the Ku80-binding domain, but not the three target amino acids for acetylation in the DNA-binding domain, is involved in the localization and accumulation of Ku70 at DSBs. Furthermore, accumulations of XRCC4 and XLF, but not that of Artemis, at DSBs are dependent on the presence of Ku70. These findings suggest that Artemis can work in not only the Ku-dependent repair process, but also the Ku-independent process at DSBs in living epithelialmore » cells.« less

Authors:
 [1];  [1];  [1]
  1. DNA Repair Gene Research, National Institute of Radiological Sciences, 4-9-1 Anagawa, Inage-ku, Chiba 263-8555 (Japan)
Publication Date:
OSTI Identifier:
22212178
Resource Type:
Journal Article
Journal Name:
Experimental Cell Research
Additional Journal Information:
Journal Volume: 317; Journal Issue: 17; Other Information: Copyright (c) 2011 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0014-4827
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ACETYLATION; BIOLOGICAL PATHWAYS; DNA; IRRADIATION; LEUCINE; LUNGS; PROTEINS; STRAND BREAKS

Citation Formats

Koike, Manabu, Yutoku, Yasutomo, Graduate School of Science, Chiba University, Yayoicho, Inage-ku, Chiba 263-8522, and Koike, Aki. Accumulation of Ku70 at DNA double-strand breaks in living epithelial cells. United States: N. p., 2011. Web. doi:10.1016/J.YEXCR.2011.07.018.
Koike, Manabu, Yutoku, Yasutomo, Graduate School of Science, Chiba University, Yayoicho, Inage-ku, Chiba 263-8522, & Koike, Aki. Accumulation of Ku70 at DNA double-strand breaks in living epithelial cells. United States. https://doi.org/10.1016/J.YEXCR.2011.07.018
Koike, Manabu, Yutoku, Yasutomo, Graduate School of Science, Chiba University, Yayoicho, Inage-ku, Chiba 263-8522, and Koike, Aki. 2011. "Accumulation of Ku70 at DNA double-strand breaks in living epithelial cells". United States. https://doi.org/10.1016/J.YEXCR.2011.07.018.
@article{osti_22212178,
title = {Accumulation of Ku70 at DNA double-strand breaks in living epithelial cells},
author = {Koike, Manabu and Yutoku, Yasutomo and Graduate School of Science, Chiba University, Yayoicho, Inage-ku, Chiba 263-8522 and Koike, Aki},
abstractNote = {Ku70 and Ku80 play an essential role in the DNA double-strand break (DSB) repair pathway, i.e., nonhomologous DNA-end-joining (NHEJ). No accumulation mechanisms of Ku70 at DSBs have been clarified in detail, although the accumulation mechanism of Ku70 at DSBs plays key roles in regulating the NHEJ activity. Here, we show the essential domains for the accumulation and function of Ku70 at DSBs in living lung epithelial cells. Our results showed that EGFP-Ku70 accumulation at DSBs began immediately after irradiation. Our findings demonstrate that three domains of Ku70, i.e., the {alpha}/{beta}, DNA-binding, and Ku80-binding domains, but not the SAP domain, are necessary for the accumulation at or recognition of DSBs in the early stage after irradiation. Moreover, our findings demonstrate that the leucine at amino acid 385 of Ku70 in the Ku80-binding domain, but not the three target amino acids for acetylation in the DNA-binding domain, is involved in the localization and accumulation of Ku70 at DSBs. Furthermore, accumulations of XRCC4 and XLF, but not that of Artemis, at DSBs are dependent on the presence of Ku70. These findings suggest that Artemis can work in not only the Ku-dependent repair process, but also the Ku-independent process at DSBs in living epithelial cells.},
doi = {10.1016/J.YEXCR.2011.07.018},
url = {https://www.osti.gov/biblio/22212178}, journal = {Experimental Cell Research},
issn = {0014-4827},
number = 17,
volume = 317,
place = {United States},
year = {Sat Oct 15 00:00:00 EDT 2011},
month = {Sat Oct 15 00:00:00 EDT 2011}
}