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Nucleic Acids Research 2005 33(7):2090-2098; doi:10.1093/nar/gki342
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Published online 11 April 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase

Nicholas S. Y. Ting, Yaping Yu, Brant Pohorelic, Susan P. Lees-Miller and Tara L. Beattie*

Department of Biochemistry and Molecular Biology, Cancer Biology Research Group, University of Calgary 3330 Hospital Drive N.W. Calgary, Alberta, Canada T2N 4N1

*To whom correspondence should be addressed. Tel: +1 403 220 8328; Fax: +1 403 283 8727; Email: tbeattie{at}ucalgary.ca

Received December 16, 2004. Revised March 4, 2005. Accepted March 18, 2005.

Maintenance of telomere integrity requires the dynamic interplay between telomerase, telomere-associated proteins and DNA repair proteins. These interactions are vital to suppress DNA damage responses and changes in chromosome dynamics that can result in aneuploidy or other transforming aberrations. The interaction between the DNA repair protein Ku and the RNA component of telomerase (TLC1) in Saccharomyces cerevisiae has been shown to be important for maintaining telomere length. Here, we sought to determine whether this interaction was conserved in higher eukaryotes. Although there is no sequence similarity between TLC1 and the RNA component (hTR) of human telomerase, we show that human Ku70/80 interacts with hTR both in vitro and in a cellular context. Specifically, Ku70/80 interacts with a 47 nt region of the 3' end of hTR, which resembles the stem–loop region of the yeast Ku70/80 binding domain on TLC1. Furthermore, utilizing immunoprecipitation/RT–PCR experiments, we show that Ku interacts with hTR in cell lines deficient in the human telomerase reverse transcriptase protein (hTERT), suggesting that this interaction does not require hTERT. These data suggest that Ku interacts directly with hTR, independent of hTERT, providing evidence for the conservation of the interaction between Ku and telomerase RNA among various species and provide significant insight into how Ku is involved in telomere maintenance in higher eukaryotes.


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