Nucleic Acids Research Advance Access published online on November 11, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp1008
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Genome Integrity, Repair and Replication |
Sumoylation of the BLM ortholog, Sgs1, promotes telomere–telomere recombination in budding yeast
1Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan and 2Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey, 08854, USA
*To whom correspondence should be addressed. Tel: 886 2 23123456 (Ext. 88294); Fax: 886 2 23915293; Email: shuchunteng{at}ntu.edu.tw
Received May 26, 2009. Revised October 14, 2009. Accepted October 16, 2009.
BLM and WRN are members of the RecQ family of DNA helicases, and in humans their loss is associated with syndromes characterized by genome instability and cancer predisposition. As the only RecQ DNA helicase in the yeast Saccharomyces cerevisiae, Sgs1 is known to safeguard genome integrity through its role in DNA recombination. Interestingly, WRN, BLM and Sgs1 are all known to be modified by the small ubiquitin-related modifier (SUMO), although the significance of this posttranslational modification remains elusive. Here, we demonstrate that Sgs1 is specifically sumoylated under the stress of DNA double strand breaks. The major SUMO attachment site in Sgs1 is lysine 621, which lies between the Top3 binding domain and the DNA helicase domain. Surprisingly, sumoylation of K621 was found to be uniquely required for Sgs1’s role in telomere–telomere recombination. In contrast, sumoylation was dispensable for Sgs1’s roles in DNA damage tolerance, supppression of direct repeat and rDNA recombination, and promotion of top3
slow growth. Our results demonstrate that although modification by SUMO is a conserved feature of RecQ family DNA helicases, the major sites of modification are located on different domains of the protein in different organisms. We suggest that sumoylation of different domains of RecQ DNA helicases from different organisms contributes to conserved roles in regulating telomeric recombination.