Article Abstract:
A study of the structure of the RuvA-Holliday junction complex through an analysis of RuvA contacts with each of the four DNA strands reveals that all four strands exhibit a foot-print of nearly 13 nt on both sides of the crossover point on all four DNA strands. No such protection is associated with the linear duplex DNA, indicating that structure specific interactions with the Holliday crossover result in the footprint. The binding of RuvA to the Holliday junction is symmetric about the crossover point, contacting all four flanking duplex arms.
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Article Abstract:
It is becoming clear that the E. coli Ruv proteins RuvA, RuvB and RuvC can form a functional complex that can be regarded as a 'resolvasome.' Electron microscopy can give an insight into the structure of the RuvAB-Holliday junction complex, in which the proteins assemble as a tripartite complex with RuvA flanked by two hexameric rings of RuvB. Both general and site-specific recombination processes use the Holliday junction as an intermediate and have developed proteins that change its structure into a near square-planar configuration.
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Article Abstract:
Research has been conducted on the DNA strand exchange which leads to the Holliday junction formation during the homologous recombination. Results indicate that the branch migration of this junction along DNA extends the heteroduplex joint length.
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