TY - JOUR
T1 - Rad52 SUMOylation affects the efficiency of the DNA repair
AU - Altmannova, Veronika
AU - Eckert-Boulet, Nadine
AU - Arneric, Milica
AU - Kolesar, Peter
AU - Chaloupkova, Radka
AU - Damborsky, Jiri
AU - Sung, Patrick
AU - Zhao, Xiaolan
AU - Lisby, Michael
AU - Krejci, Lumir
N1 - Funding Information:
Wellcome Trust International Senior Research Fellowship (WT076476); Czech Science Foundation (grants 301/09/317 and 203/09/H046); the Ministry of Education Youth and Sport of the Czech Republic [grants ME10048; MSM0021622413 and LC06030 (to L.K.), MSM0021622412 (to J.D.) and LC06010 (to R.Ch)]; the Danish Agency for Science, Technology and Innovation (to M.L.); the Villum Kann Rasmussen Foundation (to M.L.); the Lundbeck Foundation (to N.E.B.); RO1ES07061 (to P.S.); R01GM080670 grant (to X.Z.). Funding for open access charges: Wellcome Trust (WT047276).
PY - 2010/4/5
Y1 - 2010/4/5
N2 - 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 single-stranded DNA, 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.
AB - 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 single-stranded DNA, 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.
UR - https://www.scopus.com/pages/publications/77955813573
UR - https://www.scopus.com/pages/publications/77955813573#tab=citedBy
U2 - 10.1093/nar/gkq195
DO - 10.1093/nar/gkq195
M3 - Article
C2 - 20371517
AN - SCOPUS:77955813573
SN - 0305-1048
VL - 38
SP - 4708
EP - 4721
JO - Nucleic acids research
JF - Nucleic acids research
IS - 14
ER -