The repair of psoralen monoadducts by the Escherichia coli UvrABC endonuclease.

Abstract:

:We have examined the interactions of UvrABC endonuclease with DNA containing the monoadducts of 8-methoxypsoralen (8-MOP) and 4,5',8-trimethylpsoralen (TMP). The UvrA and UvrB proteins were found to form a stable complex on DNA that contains the psoralen monoadducts. Subsequent binding of UvrC protein to this complex activates the UvrABC endonuclease activity. As in the case of incision at pyrimidine dimers, a stable protein-DNA complex was observed after the incision events. For both 8-MOP and TMP, the UvrABC endonuclease incised the monoadduct-containing strand of DNA on the two sides of the monoadduct with 12 bases included between the two cuts. One incision was at the 8th phosphodiester bond on the 5' side of the modified base. The other incision was at the 5th phosphodiester bond 3' to the modified base. The UvrABC endonuclease incision data revealed that the reactivity of psoralens is 5'TpA greater than 5'ApT greater than 5'TpG.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Yeung AT,Jones BK,Capraro M,Chu T

doi

10.1093/nar/15.12.4957

subject

Has Abstract

pub_date

1987-06-25 00:00:00

pages

4957-71

issue

12

eissn

0305-1048

issn

1362-4962

journal_volume

15

pub_type

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