期刊
FEBS LETTERS
卷 585, 期 6, 页码 841-846出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.02.020
关键词
Ku; XLF; Cernunnos; Non-homologous end-joining; DNA double-strand break
资金
- National Institute of Health [CA050519, CA92584]
- MEXT, Japan
- Sagawa Foundation for Promotion of Cancer Research
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
Ku heterodimer is essential for the repair of DNA double-strand breaks (DSBs) by non-homologous end-joining (NHEJ). Ku recruits XLF, also known as Cernunnos, to DSBs. Here we report domain analyses of Ku-XLF interaction. The heterodimeric domain of Ku was found to be sufficient for the recruitment of XLF to DSBs and for the interaction of Ku with XLF. A small C-terminal deletion of XLF completely abolished recruitment of XLF to DSBs and Ku-XLF interaction. This deletion also led to marked reduction of XLF-XRCC4 interaction although the XRCC4-binding site on the XLF N-terminal domain remained intact. These results demonstrate the significance of Ku-XLF interaction in the molecular assembly of NHEJ factors. Structured summary of protein interactions: XLF physically interacts with XRCC4 and Ku by anti tag coimmunoprecipitation (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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