Smc5/6 Mediated Sumoylation of the Sgs1-Top3-Rmi1 Complex Promotes Removal of Recombination Intermediates

Publication date: Available online 30 June 2016
Source:Cell Reports
Author(s): Jaclyn N. Bonner, Koyi Choi, Xiaoyu Xue, Nikko P. Torres, Barnabas Szakal, Lei Wei, Bingbing Wan, Meret Arter, Joao Matos, Patrick Sung, Grant W. Brown, Dana Branzei, Xiaolan Zhao
Timely removal of DNA recombination intermediates is critical for genome stability. The DNA helicase-topoisomerase complex, Sgs1-Top3-Rmi1 (STR), is the major pathway for processing these intermediates to generate conservative products. However, the mechanisms that promote STR-mediated functions remain to be defined. Here we show that Sgs1 binds to poly-SUMO chains and associates with the Smc5/6 SUMO E3 complex in yeast. Moreover, these interactions contribute to the sumoylation of Sgs1, Top3, and Rmi1 upon the generation of recombination structures. We show that reduced STR sumoylation leads to accumulation of recombination structures, and impaired growth in conditions when these structures arise frequently, highlighting the importance of STR sumoylation. Mechanistically, sumoylation promotes STR inter-subunit interactions and accumulation at DNA repair centers. These findings expand the roles of sumoylation and Smc5/6 in genome maintenance by demonstrating that they foster STR functions in the removal of recombination intermediates.

Graphical abstract

Teaser

Bonner et al. show that the Smc5/6 SUMO ligase complex interacts with and promotes the sumoylation of the DNA helicase Sgs1 and its partner proteins Top3 and Rmi1. Sgs1-Top3-Rmi1 (STR) sumoylation fosters the removal of recombination intermediates, in part by stimulating STR inter-subunit interaction and STR accumulation at DNA repair centers.


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