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J. Biol. Chem., Vol. 276, Issue 12, 9071-9076, March 23, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/12/9071    most recent M008918200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yang, I.-Y. Articles by Moriya, M. Search for Related Content PubMed PubMed Citation Articles by Yang, I.-Y. Articles by Moriya, M.

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

From the  Laboratory of Chemical Biology, Department of Pharmacological Sciences and ^¶ Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-8651

Acrolein, a reactive ,-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-(-D-2'-deoxyribofuranosyl)-5,6,7,8-tetrahydropyrido[3,2-a]purine-9-one (-OH-PdG). The cellular processing and mutagenic potential of -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 this adduct is excised by nucleotide excision repair. The apparent level of inhibition of DNA synthesis is ~70% in Escherichia coli recA, uvrA. The block to DNA synthesis can be overcome partially by recA-dependent recombination repair. Targeted G  T transversions were observed at a frequency of 7 × 10⁴/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 polymerase I catalyzes error-prone synthesis, preferentially incorporating dAMP and dGMP opposite -OH-PdG. We conclude from this study that DNA polymerase III catalyzes translesion synthesis across -OH-PdG in an error-free manner. Nucleotide excision repair, recombination repair, and highly accurate translesion synthesis combine to protect E. coli from the potential genotoxicity of this DNA adduct.

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