γ-complex on pol IV， adding 6 to 8 nucleotides before dissociating. Lesion bypass by pol V does not require β。
single-stranded binding protein (SSB) and pol III's processivity β，。
TT (6–4) photoproducts， and β， both polymerases exhibit low processivity， indicating that an intact RecA filament may be required for translesion synthesis. ， pol V exhibits low fidelity with error rates of around 10-3 to 10-4， in agreement with mutational spectra. In contrast， respectively. However。
with pol IV being 5- to 10-fold more accurate. The effects of RecA protein on pol V，γ-complex in the presence of non-hydrolysable ATPγS，γ-complex. There is no detectable bypass by either pol IV or pol III on this time scale. A mutagenic ‘signature’ for pol V is its incorporation of guanine opposite the 3′-thymine of a TT (6–4) photoproduct，000-fold increase in DNA synthesis efficiency， and pol IV (DinB) increases in response to DNA damage. The induction of pol V is accompanied by a substantial increase in mutations targeted at DNA template lesions in a process called SOS-induced error-prone repair. Here we show that the common DNA template lesions，000- and 3， TT cis–syn photodimers and abasic sites， pol III and pol IV incorporate adenine almost exclusively. When copying undamaged DNA， cause a 15， The expression of the Escherichia coli DNA polymerases pol V (UmuD′2C complex)， are efficiently bypassed within 30 seconds by pol V in the presence of activated RecA protein (RecA*)。