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

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
;  [1]
  1. Institute for Cancer Research, Philadelphia, PA (USA)

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.

OSTI ID:
5601909
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 85:22; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English