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Nucleic Acids Research 2006 34(2):506-516; doi:10.1093/nar/gkj452
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Published online 20 January 2006

© The Author 2006. 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}oxfordjournals.org

Article

Evidence that the S.cerevisiae Sgs1 protein facilitates recombinational repair of telomeres during senescence

Mahrukh Azam1, Julia Y. Lee1, Veena Abraham1, Rebecca Chanoux2, Kimberly A. Schoenly2 and F. Brad Johnson1,2,*

1Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine Philadelphia, PA, USA 2Cell and Molecular Biology Graduate Program, University of Pennsylvania School of Medicine Philadelphia, PA, USA

*To whom correspondence should be addressed. Tel: +1 215 573 5037; Fax: +1 215 573 6317; Email: johnsonb{at}mail.med.upenn.edu

Received October 30, 2005. Revised December 22, 2005. Accepted January 4, 2006.

RecQ DNA helicases, including yeast Sgs1p and the human Werner and Bloom syndrome proteins, participate in telomere biology, but the underlying mechanisms are not fully understood. Here, we explore the protein sequences and genetic interactors of Sgs1p that function to slow the senescence of telomerase (tlc1) mutants. We find that the S-phase checkpoint function of Sgs1p is dispensable for preventing rapid senescence, but that Sgs1p sequences required for homologous recombination, including the helicase domain and topoisomerase III interaction domain, are essential. sgs1 and rad52 mutations are epistatic during senescence, indicating that Sgs1p participates in a RAD52-dependent recombinational pathway of telomere maintenance. Several mutations that are synthetically lethal with sgs1 mutation and which individually lead to genome instability, including mus81, srs2, rrm3, slx1 and top1, do not speed the senescence of tlc1 mutants, indicating that the rapid senescence of sgs1 tlc1 mutants is not caused by generic genome instability. However, mutations in SLX5 or SLX8, which encode proteins that function together in a complex that is required for viability in sgs1 mutants, do speed the senescence of tlc1 mutants. These observations further define roles for RecQ helicases and related proteins in telomere maintenance.

Present address: Mahrukh Azam, Department of Chemistry, West Chester University, West Chester, PA, USA

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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