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Figure 6.
Figure 6 Model for RecOR recognition of stalled replication
forks. Whereas the role of RecF in this process is still
unclear, it is known to associate with DNA in an ATP-dependent
fashion. Upon binding of RecOR to ssDNA–dsDNA junctions (step
2), we propose that interactions with RecF, SSB and/or DNA may
cause a structural rearrangement of RecOR (e.g. one RecO and two
RecR molecules may dissociate from the RecOR complex).
RecF-dependent ATP hydrolysis may provide the necessary energy
for this reorganisation (step 3) resulting in the formation of a
stable complex between RecOR and the stalled replication fork
(step 4). As a consequence, the assembled RecOR complex may
initiate the displacement of SSB and thus facilitate the loading
of RecA onto ssDNA, allowing for homologous recombination to
take place (step 5).
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