RecA-DNA filament topology: the overlooked alternative of an unconventional syn-syn duplex intermediate.
The helical filaments of RecA protein mediate strand exchange for homologous recombination, but the paths of the interacting DNAs have yet to be determined. Although this interaction is commonly limited to three strands, it is reasoned here that the intrinsic symmetry relationships of quadruplex topology are superior in explaining a range of observations. In particular, this topology suggests the potential of post-exchange base pairing in the unorthodox configuration of syn-syn glycosidic bonds between the nucleotide bases and the pentose rings in the sugar-phosphate backbone, which would transiently be stabilized by the external scaffolding of the RecA protein filament.
Egel
Richard
R
Institute of Molecular Biology and Physiology, University of Copenhagen, Ole Maaløe Vej 5, DK-2100 Copenhagen Ø, Denmark. regel@my.molbio.ku.dk
D000818:Animals; D020029:Base Pairing; D004247:DNA / Q000235:genetics*; D006801:Humans; D009690:Nucleic Acid Conformation; D011938:Rec A Recombinases / Q000235:genetics*; D011995:Recombination, Genetic
D004247:DNA; D011938:Rec A Recombinases