Homologous recognition by RecA protein using non-equivalent three DNA-strand-binding sites.
A key step in homologous recombination is the formation of a heteroduplex joint between double-stranded DNA and single-stranded DNA by the homologous pairing and strand-exchange, and this step is also important in recombinational repair of damaged DNA in various organisms. The homologous pairing and the strand-exchange are promoted in vivo and in vitro by RecA protein of Escherichia coli or its homologues of bacteria, virus, and lower and higher eukaryotes. A central question on the mechanism of homologous recombination is how RecA protein (and its homologues) recognizes homologous sequences between single-stranded DNA and double-stranded DNA. Recent studies suggest that RecA protein promotes homologous recognition between these DNA molecules by the formation of a transient and additional pairing of identical sequences via non-Watson-Crick interactions to the Watson-Crick-type duplex DNA, and that RecA protein uses three non-equivalent DNA-strand-binding sites in this reaction.
Kurumizaka
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Laboratory of Cellular & Molecular Biology, Institute of Physical and Chemical Research (RIKEN), Saitama.
Shibata
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D000818:Animals; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011938:Rec A Recombinases / Q000737:chemistry / Q000378:metabolism*
C051802:triplex DNA; D004247:DNA; D011938:Rec A Recombinases