Rad52 multimerization is important for its nuclear localization in Saccharomyces cerevisiae

Iben Plate, Line Albertsen, Michael Lisby, Swee C.L. Hallwyl, Qi Feng, Changhyun Seong, Rodney Rothstein, Patrick Sung, Uffe H. Mortensen

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


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 NLSRad52 sort efficiently to the nucleus. Based on the results we propose a model where the additive effect of multiple NLSRad52 sequences in a Rad52 ring-structure ensures efficient nuclear localization of Rad52.

Original languageEnglish (US)
Pages (from-to)57-66
Number of pages10
JournalDNA Repair
Issue number1
StatePublished - Jan 1 2008
Externally publishedYes


  • DNA repair
  • Homologous recombination
  • NLS
  • Nuclear localization
  • Rad52
  • S. cerevisiae

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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