Abstract
In recombinational DNA repair, nearly identical sequences in chromosomes are found and swapped. Structures of the RecA–DNA complexes involved provide insight into the mechanism and energetics of this universal process. One way of reversing DNA damage involves homologous pairing of an undamaged DNA with a damaged DNA, a process mediated by a class of proteins known as strand-exchange proteins. Chen et al. now present a 'holy grail' of the DNA repair field: the structure of the E. coli strand-exchange protein, RecA, bound to one and two DNA molecules. More than a dozen crystal structures of bacterial, archaebacterial and eukaryotic RecA-family members have been determined previously, but because RecA forms a filament on DNA, no crystal structures of RecA–DNA complexes were available. The new study avoids the problem of crystallizing a polymer by engineering RecA–DNA complexes that represent finite segments of the filament.
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