Rad52 multimerization is important for its nuclear localization in Saccharomyces cerevisiae
| Autor: | Rodney Rothstein, Michael Lisby, Uffe Hasbro Mortensen, Swee Chuang Lim Hallwyl, Iben Plate, Line Albertsen, Qi Feng, Changhyun Seong, Patrick Sung |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
DNA repair
Protein subunit Molecular Sequence Data Nuclear Localization Signals genetic processes Saccharomyces cerevisiae RAD52 Importin Biology Biochemistry Article Biopolymers NLS Amino Acid Sequence Molecular Biology Cell Nucleus Sequence Homology Amino Acid fungi Cell Biology biology.organism_classification Molecular biology Rad52 DNA Repair and Recombination Protein Cell biology enzymes and coenzymes (carbohydrates) Microscopy Fluorescence Nuclear transport Nuclear localization sequence DNA Damage Plasmids |
| Zdroj: | DNA Repair. 7:57-66 |
| ISSN: | 1568-7864 |
| DOI: | 10.1016/j.dnarep.2007.07.016 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect