Repair of 4,5',8-trimethylpsoralen monoadducts and cross-links by the Escherichia coli UvrABC endonuclease

Using an oligonucleotide model substrate, the authors observed two unusual mechanisms of UvrABC endonuclease in the repair of 4,5',8-trimethylpsoralen monaddducts and cross-links. (i) UvrABC endonuclease usually incises a psoralen monadduct only on the damaged strand. However, for one of the monadducts they studied, incision on the complementary undamaged strand was also observed at a very low frequency, as though the adduct were on the thymine across from the damaged strand. Although the details of the erroneous incision are not yet know, such erroneous incision is potentially mutagenic. (ii) In cross-link repair, they observed that the UvrABC endonuclease incises the cross-linked DNA on either the furan side strand or the pyrone side strand. The incisions are not equally efficient. These data suggest that the structure of a psoralen cross-link, as seen by a repair enzyme, varies with the DNA sequence