Nucleic Acids Research Advance Access originally published online on November 15, 2006
Nucleic Acids Research 2006 34(21):6327-6336; doi:10.1093/nar/gkl786
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Nucleic Acids Research, 2006, Vol. 34, No. 21 6327-6336
© 2006 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 |
The telomerase-recruitment domain of the telomere binding protein Cdc13 is regulated by Mec1p/Tel1p-dependent phosphorylation
1 Department of Microbiology, College of Medicine, National Taiwan University Taipei, Taiwan 2 Institute of Biopharmaceutical Science, National Yang-Ming University Taipei, Taiwan 3 Institute of Internal Medicine, National Taiwan University Hospital Taipei, Taiwan
*To whom correspondence should be addressed. Tel: +886 2 2312 3456, ext. 8282; Fax: +886 2 23915293; Email: scteng{at}ha.mc.ntu.edu.tw
Received August 23, 2006. Revised September 28, 2006. Accepted September 28, 2006.
The DNA damage-responsive protein kinases ATM and ATR phosphorylate SQ/TQ motifs that lie in clusters in most of their in vivo targets. Budding yeast Cdc13p contains two clusters of SQ/TQ motifs, suggesting that it might be a target of Mec1p/Tel1p (yeast ATR/ATM). Here we demonstrated that the telomerase recruitment domain of Cdc13p is phosphorylated by Mec1p and Tel1p. Gel analysis showed that Cdc13p contains a Mec1/Tel1-dependent post-translational modification. Using an immunoprecipitate (IP)-kinase assay, we showed that Mec1p phosphorylates Cdc13p on serine 225, 249, 255 and 306, and Tel1p phosphorylates Cdc13p on serine 225, 249 and 255 in vitro. Phenotypic analysis in vivo revealed that the mutations in the Cdc13p SQ motifs phosphorylated by Mec1p and Tel1p caused multiple telomere and growth defects. In addition, normal telomere length and growth could be restored by expressing a Cdc13–Est1p hybrid protein. These results demonstrate the telomerase recruitment domain of Cdc13p as an important new telomere-specific target of Mec1p/Tel1p.
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