Nucleic Acids Research Advance Access originally published online on March 27, 2007
Nucleic Acids Research 2007 35(7):2321-2332; doi:10.1093/nar/gkm127
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Nucleic Acids Research, 2007, Vol. 35, No. 7 2321-2332
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Conserved interactions of the splicing factor Ntr1/Spp382 with proteins involved in DNA double-strand break repair and telomere metabolism
1Department of Dermatology, University of Cologne, D-50924 Cologne, Germany, 2Centre for Biomedicine, University of Basel, CH-4058 Basel, Switzerland, 3Institute of Molecular Cancer Research, University of Zürich, CH-8008 Zürich, Switzerland and 4Friedrich Miescher Institute for Biomedical Research, CH-4058 Basel, Switzerland
*To whom correspondence should be addressed. Tel: ++49-221-478-7341; Fax: ++49-221-478-5949; Email: gernot.herrmann{at}uni-koeln.de
Received November 22, 2006. Revised February 14, 2007. Accepted February 15, 2007.
The ligation of DNA double-strand breaks in the process of non-homologous end-joining (NHEJ) is accomplished by a heterodimeric enzyme complex consisting of DNA ligase IV and an associated non-catalytic factor. This DNA ligase also accounts for the fatal joining of unprotected telomere ends. Hence, its activity must be tightly controlled. Here, we describe interactions of the DNA ligase IV-associated proteins Lif1p and XRCC4 of yeast and human with the putatively orthologous G-patch proteins Ntr1p/Spp382p and NTR1/TFIP11 that have recently been implicated in mRNA splicing. These conserved interactions occupy the DNA ligase IV-binding sites of Lif1p and XRCC4, thus preventing the formation of an active enzyme complex. Consistently, an excess of Ntr1p in yeast reduces NHEJ efficiency in a plasmid ligation assay as well as in a chromosomal double-strand break repair (DSBR) assay. Both yeast and human NTR1 also interact with PinX1, another G-patch protein that has dual functions in the regulation of telomerase activity and telomere stability, and in RNA processing. Like PinX1, NTR1 localizes to telomeres and associates with nucleoli in yeast and human cells, suggesting a function in localized control of DSBR.
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