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A more recent version of this article appeared on March 16, 2001
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Papers In Press, published online ahead of print December 21, 2000
J. Biol. Chem, 10.1074/jbc.M008918200
Submitted on September 29, 2000
Revised on December 5, 2000
Accepted on December 20, 2000

Responses to the major acrolein-derived deoxyguanosine adduct in Escherichia coli

In-Young Yang, Munfarah Hossain, Holly Miller, Sonia Khullar, Francis Johnson, Arthur Grollman, and Masaaki Moriya

Pharmacological Sciences, SUNY at Stony Brook, Stony Brook, NY 11794-8651

Corresponding Author: maki{at}pharm.sunysb.edu

Acrolein, a reactive alpha ,beta -unsaturated aldehyde found ubiquitously in the environment and formed endogenously in mammalian cells, reacts with DNA to form an exocyclic DNA adduct, 3H-8-hydroxy-3-(beta -D-2'-deoxyribofuranosyl)-5,6,7,8-tetrahydropyrido[3,2-a]purine-9-one (gamma -OH-PdG). The cellular processing and mutagenic potential of gamma -OH-PdG have been examined, using a site-specific approach in which a single adduct is embedded in double strand plasmid DNA. Analysis of progeny plasmid reveals that gamma -OH-PdG inhibits DNA synthesis by approximately 70% and is excised by nucleotide excision repair. The block to DNA synthesis can be overcome partially by recA-dependent recombination repair. Targeted G to T transversions were observed at a frequency of 7x10-4/ translesion synthesis. Inactivation of polB , dinB and umuD,C genes coding for "SOS" DNA polymerases did not affect significantly the efficiency or fidelity of translesion synthesis. In vitro primer extension experiments revealed that the Klenow fragment of pol I catalyzes error-prone synthesis, preferentially incorporating dAMP and dGMP opposite gamma -OH-PdG. We conclude from this study that the DNA polymerase III catalyzes translesion synthesis across gamma -OH-PdG in an error-free manner. Nucleotide excision repair, recombination repair and highly accurate translesion synthesis combine to protect Escherichia coli from the potential genotoxicity of this DNA adduct.


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