TY - JOUR

T1 - Rad52 SUMOylation affects the efficiency of the DNA repair

T2 - [Inkl. Corrigendum]

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 - Corrigendum 1: 10.1093/nar/gks252 Link: https://academic.oup.com/nar/article/40/8/3775/2411843 Corrigendum 2: 10.1093/nar/gkad065 Link: https://academic.oup.com/nar/article/51/4/1998/7009120

PY - 2010

Y1 - 2010

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.

KW - DNA Repair

KW - DNA, Single-Stranded

KW - Lysine

KW - Protein Structure, Tertiary

KW - Rad51 Recombinase

KW - Rad52 DNA Repair and Recombination Protein

KW - Recombination, Genetic

KW - Replication Protein A

KW - SUMO-1 Protein

KW - Saccharomyces cerevisiae Proteins

U2 - 10.1093/nar/gkq195

DO - 10.1093/nar/gkq195

M3 - Journal article

C2 - 20371517

VL - 38

SP - 4708

EP - 4721

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 14

ER -