Abstract
The Escherichia coli protein DinB plays an important role in the SOS response to DNA damage. DinB is a member of the Y‐family of polymerases which serve to synthesize DNA from a damaged bulky template in a process known as translesion synthesis (TLS). DinB in particular is the only Y‐family polymerase that is conserved throughout all domains of life. In addition to synthesizing DNA across from lesions, DinB is associated with ‐1 frameshift mutations that are particularly lethal. RecA and UmuD have already been shown to modulate DinB activity preventing the ‐1 frameshift mutation during TLS in vitro, however no such study has been carried out in vivo. By constructing DinB, RecA, and UmuD fluorescent fusion proteins, the localization and prevalence of these proteins will be able to be monitored in vivo thus proving or disproving the in vitro findings that DinB, RecA and UmuD form a multi‐protein complex preventing mutagenesis during TLS.
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