Yeast RAD51 gene functions in genetic recombination and DNA double-strand break repair. In vitro, in the presence of ATP and replication protein A, RAD51 protein pairs single-stranded DNA (ssDNA) with homologous double-stranded DNA (dsDNA) and catalyzes strand exchange between the synapsed DNA partners. Electron microscopic analyses show that RAD51 forms helical filaments on both ssDNA and dsDNA, in which the DNA is highly extended. However, results presented here indicate that only the RAD51-ssDNA nucleoprotein filament is functionally relevant. Strand exchange is arrested when heterology is encountered in the duplex partner, and analysis of the configuration of the terminal joint thus formed reveals that pairing and strand exchange initiate at the 5' end of the complementary strand in the linear duplex, a reaction polarity opposite to that of the bacterial prototype RecA.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Annotation Extension||Reference|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Assay||Construct||Conditions||Strain Background||Reference|