By Frederick W. Alt
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Analogous to Vpr‐mediated transport of the preintegration complex during the viral life cycle, a Vpr‐like host protein might exist that recruits UNG to the CSR machinery. Hence, the WXXF motif is critical for preserving the CSR function of UNG (Fig. 4). In summary, initial studies demonstrated that S region breaks can be detected in the absence of UNG, and the catalytic activity of UNG is dispensable for CSR. Subsequent studies using N‐terminal UNG truncations revealed that the role of UNG in the replication‐coupled repair pathway is not mandatory for CSR.
Series of N‐terminal truncations and PCNA‐binding defective mutants were generated, and their CSR rescue activities were examined in ungÀ/À B cells. N‐terminal truncation of the first 86 residues of UNG showed efficient CSR rescue activity comparable to full‐length UNG (Table 1), whereas N‐terminal deletions of more than 96 residues did not rescue CSR activity in ungÀ/À B cells. Consistent with this observation, CSR rescue was also detected using E. coli UNG, which lacks the mammalian‐type N‐terminus and is solely composed of the catalytic domain.
Mutations preferentially convert C/G to T/A, concordant with the idea that AID directly deaminates C in DNA to generate U. The mutation rate is enhanced under conditions of uracil DNA glycosylase (UNG) deficiency. These observations led to proposal of the DNA deamination model, in which AID directly deaminates C in target DNA to generate U:G mismatch sites (Fig. 4). Mismatch sites are recognized either by base excision repair (BER) enzymes, including UNG and apyrimidinic endonuclease, or by mismatch repair proteins Msh2/Msh6 that induce the patch repair system, resulting in DNA strand cleavage.