Rad52 multimerization is important for its nuclear localization in Saccharomyces cerevisiae.

TY - JOUR

T1 - Rad52 multimerization is important for its nuclear localization in Saccharomyces cerevisiae.

AU - Plate, Iben

AU - Albertsen, Line

AU - Lisby, Michael

AU - Hallwyl, Swee C L

AU - Feng, Qi

AU - Seong, Changhyun

AU - Rothstein, Rodney

AU - Sung, Patrick

AU - Mortensen, Uffe H

PY - 2007

Y1 - 2007

N2 - Rad52 is essential for all homologous recombination and DNA double strand break repair events in Saccharomyces cerevisiae. This protein is multifunctional and contains several domains that allow it to interact with DNA as well as with different repair proteins. However, it has been unclear how Rad52 enters the nucleus. In the present study, we have used a combination of mutagenesis and sequence analysis to show that Rad52 from S. cerevisiae contains a single functional pat7 type NLS essential for its nuclear localization. The region containing the NLS seems only to be involved in nuclear transport as it plays no role in repair of MMS-induced DNA damage. The NLS in Rad52 is weak, as monomeric protein species that harbor this NLS are mainly located in the cytosol. In contrast, multimeric protein complexes wherein each subunit contains a single NLS(Rad52) sort efficiently to the nucleus. Based on the results we propose a model where the additive effect of multiple NLS(Rad52) sequences in a Rad52 ring-structure ensures efficient nuclear localization of Rad52.

AB - Rad52 is essential for all homologous recombination and DNA double strand break repair events in Saccharomyces cerevisiae. This protein is multifunctional and contains several domains that allow it to interact with DNA as well as with different repair proteins. However, it has been unclear how Rad52 enters the nucleus. In the present study, we have used a combination of mutagenesis and sequence analysis to show that Rad52 from S. cerevisiae contains a single functional pat7 type NLS essential for its nuclear localization. The region containing the NLS seems only to be involved in nuclear transport as it plays no role in repair of MMS-induced DNA damage. The NLS in Rad52 is weak, as monomeric protein species that harbor this NLS are mainly located in the cytosol. In contrast, multimeric protein complexes wherein each subunit contains a single NLS(Rad52) sort efficiently to the nucleus. Based on the results we propose a model where the additive effect of multiple NLS(Rad52) sequences in a Rad52 ring-structure ensures efficient nuclear localization of Rad52.

U2 - 10.1016/j.dnarep.2007.07.016

DO - 10.1016/j.dnarep.2007.07.016

M3 - Journal article

C2 - 17888746

SN - 1568-7864

VL - 7

SP - 57

EP - 66

JO - DNA Repair

JF - DNA Repair

IS - 1

ER -