Nucleic Acids Research · 1994 · 12 citations · 18 references
The helical filament formed by RecA protein on single-stranded DNA plays an important role in homologous recombination and pairs with a complementary single strand or homologous duplex DNA. The RecA nucleoprotein filament also recognizes an identical single strand. The chimeric protein, RecAc38, forms a nucleoprotein filament that recognizes a complementary strand but is defective in recognition of duplex DNA, and is associated with phenotypic defects in repair and recombination. As described here, RecAc38 nucleoprotein filament is also defective in recognition of an identical strand, either when the filament has within it a single strand or duplex DNA. A model that postulates three DNA binding sites rationalizes these observations and suggests that the third binding site mediates non-Watson-Crick interactions that are instrumental in recognition of homology in duplex DNA.
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Douglas K. Bishop, Demian Park, Liuzhong Xu et al. · Cell · 1992 · 1.2K citations
Meiosis-specific Yeast Homolog, Synaptonemal Complex Formation, E. Coli Reca +10
Similarity of the Yeast RAD51 Filament to the Bacterial RecA Filament
Tomoko Ogawa, Xiong Yu, Akira Shinohara et al. · Science · 1993 · 666 citations
Takahiro Shibata, Chandan Dasgupta, Richard P. Cunningham et al. · Proceedings of the National Academy of Sciences · 1979 · 383 citations · Full text