Publication details

 

Rad52 SUMOylation affects the efficiency of the DNA repair

Basic information
Original title:Rad52 SUMOylation affects the efficiency of the DNA repair
Authors:Veronika Altmannová, Nadine Eckert-Boulet, Milica Arneric, Peter Kolesár, Radka Chaloupková, Jiří Damborský, Patrick Sung, Xiaolan Zhao, Michael Lisby, Lumír Krejčí
Further information
Citation:ALTMANNOVÁ, Veronika, Nadine ECKERT-BOULET, Milica ARNERIC, Peter KOLESÁR, Radka CHALOUPKOVÁ, Jiří DAMBORSKÝ, Patrick SUNG, Xiaolan ZHAO, Michael LISBY a Lumír KREJČÍ. Rad52 SUMOylation affects the efficiency of the DNA repair. Nucleic Acids Research, Oxford University Press, 2010, roč. 38, č. 6. ISSN 0305-1048.Export BibTeX
@article{874878,
author = {Altmannová, Veronika and EckertandBoulet, Nadine and Arneric, Milica and Kolesár, Peter and Chaloupková, Radka and Damborský, Jiří and Sung, Patrick and Zhao, Xiaolan and Lisby, Michael and Krejčí, Lumír},
article_number = {6},
keywords = {DNA repair; DNA damage; replication; genomic instability},
language = {eng},
issn = {0305-1048},
journal = {Nucleic Acids Research},
title = {Rad52 SUMOylation affects the efficiency of the DNA repair},
volume = {38},
year = {2010}
}
Original language:English
Field:Biochemistry
Type:Article in Periodical
Keywords:DNA repair; DNA damage; replication; genomic instability

Homologous recombination (HR) plays a vital role in DNA metabolic processes including meiosis, DNA repair, DNA replication, and rDNA homeostasis. HR defects can lead to pathological outcomes, including genetic diseases and cancer. Recent studies suggest that the post-translational modification by the small ubiquitin-like modifier (SUMO) protein plays an important role in mitotic and meiotic recombination. However, the precise role of SUMOylation during recombination is still unclear. Here, we characterize the effect of SUMOylation on the biochemical properties of the Saccharomyces cerevisiae recombination mediator protein Rad52. Interestingly, Rad52 SUMOylation is enhanced by ssDNA, and we show that SUMOylation of Rad52 also inhibits its DNA binding and annealing activities. The biochemical effects of SUMO modification in vitro are accompanied by a shorter duration of spontaneous Rad52 foci in vivo and a shift in spontaneous mitotic recombination from single-strand annealing to gene conversion events in the SUMO-deficient Rad52 mutants. Taken together, our results highlight the importance of Rad52 SUMOylation as part of a quality control mechanism regulating the efficiency of recombination and DNA repair.

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