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Isolation of a bacterial enzyme which releases adenine containing photoproducts from UV-irradiated DNA

Conference · · FASEB Journal (Federation of American Societies for Experimental Biology); (United States)
OSTI ID:5375445
; ;  [1]
  1. West Virginia Univ., Morgantown (United States)

It is generally assumed that DNA purines are relativity inert to photochemical alterations. However, several purine photoproducts have been characterized, including two distinct adenine dimers. Using UV-irradiated poly(dA)-poly(dT) labeled with (8-{sup 3}H dATP), as a substrate, an enzymatic activity for adenine-containing photoproducts was isolated from E. coli. The enzymatic activity specific for UV-irradiated poly(dA)-poly(dT) was separated from other UV-DNA incising activities by ion-exchange chromatography. The partially purified enzyme releases TCA-soluble material from UV-irradiated poly(dA)-poly(dT). The enzyme does not release radioactive material from poly(dA)-poly(dT) radiolabeled with (methyl-{sup 3}H)dTTP. DNA sequence analysis, has shown that the partially purified enzyme incises UV-irradiated DNA adjacent to adenines in regions of the substrate containing multiple adenines. These data indicate that the enzymatic activity is directed against adenine photoproducts. Since the radiolabel is retained upon UV-irradiation of the polynucleotide, this suggests that the structure of the recognized photoproduct is not 8,8-adenine dehydrodimer. The nature of the enzyme-released photoproduct is currently under investigation.

OSTI ID:
5375445
Report Number(s):
CONF-9104107--
Journal Information:
FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Journal Name: FASEB Journal (Federation of American Societies for Experimental Biology); (United States) Vol. 5:4; ISSN FAJOE; ISSN 0892-6638
Country of Publication:
United States
Language:
English