Carcinogenesis, Vol 19, 1339-1343, Copyright © 1998 by Oxford University Press
B Hang, A Chenna, J Sagi and B Singer
We report here that the newly synthesized DNA adduct, 1,N6-benzetheno- dA
(pBQ-dA), in defined oligonucleotides [Chenna and Singer, Chem. Res.
Toxicol., 8, 865-874], is a substrate for the major human AP endonuclease,
HAP1, and the Escherichia coli AP endonucleases, exonuclease III and
endonuclease IV. The mechanism of cleavage is identical to that reported
previously for 3,N4-benzetheno-dC (pBQ-dC) and leads to a phosphodiester
bond cleavage 5' to the adduct. There are, however, significant differences
in the rate of cleavage of this adduct by these enzymes. The two bacterial
AP endonucleases are both much more efficient than the human repair enzyme.
In addition, using two random oligodeoxynucleotide sequences containing a
single pBQ-dA, exonuclease III and endonuclease IV are similarly active,
while HAP1 shows a distinct sequence preference of approximately 10-fold in
efficiency of cleavage. The repair of this adduct by the three recombinant
enzymes is further confirmed by using both active site mutant HAP1 proteins
and by E.coli mutant strains lacking exonuclease III and/ or endonuclease
IV. This sequence-dependent repair of pBQ-dA by HAP1 may play an important
role in modulating benzene-induced carcinogenesis.
ARTICLES
Differential cleavage of oligonucleotides containing the benzene- derived adduct, 1,N6-benzetheno-dA, by the major human AP endonuclease HAP1 and Escherichia coli exonuclease III and endonuclease IV
Donner Laboratory, Lawrence Berkeley National Laboratory, University of California, Berkeley 94720, USA.
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