Molecular Anatomy of the Recombination Mediator Function of Saccharomyces cerevisiae Rad52

Autor: Uffe Hasbro Mortensen, Changhyun Seong, Peter Chi, Patrick Sung, Lumir Krejci, Iben Plate, Idina Shi, Michael G. Sehorn, Binwei Song
Rok vydání: 2008
Předmět:
Saccharomyces cerevisiae Proteins
DNA repair
genetic processes
RAD52
Saccharomyces cerevisiae
RAD51
Biology
Biochemistry
Protein filament
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Replication Protein A
DNA Breaks
Double-Stranded
DNA
Fungal
Molecular Biology
Replication protein A
030304 developmental biology
Recombination
Genetic
0303 health sciences
Genetic Complementation Test
fungi
Cell Biology
biology.organism_classification
Molecular biology
Protein Structure
Tertiary
Rad52 DNA Repair and Recombination Protein
Cell biology
Microscopy
Electron
enzymes and coenzymes (carbohydrates)
chemistry
DNA: Replication
Repair
Recombination
and Chromosome Dynamics
Mutant Proteins
Rad51 Recombinase
Homologous recombination
030217 neurology & neurosurgery
DNA
Protein Binding
Zdroj: Journal of Biological Chemistry. 283:12166-12174
ISSN: 0021-9258
DOI: 10.1074/jbc.m800763200
Popis: A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is thought to rely on the interactions of Rad52 with Rad51, the ssDNA-binding protein RPA, and ssDNA. The N-terminal region of Rad52, which has DNA binding activity and an oligomeric structure, is thought to be crucial for mediator activity and recombination. Unexpectedly, we find that the C-terminal region of Rad52 also harbors a DNA binding function. Importantly, the Rad52 C-terminal portion alone can promote Rad51 presynaptic filament assembly. The middle portion of Rad52 associates with DNA-bound RPA and contributes to the recombination mediator activity. Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Δ327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Our results provide a mechanistic framework for rationalizing the multi-faceted role of Rad52 in recombination and DNA repair.
Databáze: OpenAIRE
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