NDLI: Translesion synthesis past acrolein-derived DNA adducts by human mitochondrial DNA polymerase Î³.

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Translesion synthesis past acrolein-derived DNA adducts by human mitochondrial DNA polymerase Î³.

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Translesion synthesis past acrolein-derived DNA adducts by human mitochondrial DNA polymerase Î³.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Minko, Irina G. Lloyd, R. Stephen Kasiviswanathan, Rajesh Copeland, William C.
Description	Author Affiliation: Kasiviswanathan R ( Mitochondrial DNA Replication Group, Laboratory of Molecular Genetics, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA.)
Abstract	Acrolein, a mutagenic aldehyde, is produced endogenously by lipid peroxidation and exogenously by combustion of organic materials, including tobacco products. Acrolein reacts with DNA bases forming exocyclic DNA adducts, such as Î³-hydroxy-1,N(2)-propano-2'-deoxyguanosine (Î³-HOPdG) and Î³-hydroxy-1,N(6)-propano-2'-deoxyadenosine (Î³-HOPdA). The bulky Î³-HOPdG adduct blocks DNA synthesis by replicative polymerases but can be bypassed by translesion synthesis polymerases in the nucleus. Although acrolein-induced adducts are likely to be formed and persist in mitochondrial DNA, animal cell mitochondria lack specialized translesion DNA synthesis polymerases to tolerate these lesions. Thus, it is important to understand how pol Î³, the sole mitochondrial DNA polymerase in human cells, acts on acrolein-adducted DNA. To address this question, we investigated the ability of pol Î³ to bypass the minor groove Î³-HOPdG and major groove Î³-HOPdA adducts using single nucleotide incorporation and primer extension analyses. The efficiency of pol Î³-catalyzed bypass of Î³-HOPdG was low, and surprisingly, pol Î³ preferred to incorporate purine nucleotides opposite the adduct. Pol Î³ also exhibited â ¼2-fold lower rates of excision of the misincorporated purine nucleotides opposite Î³-HOPdG compared with the corresponding nucleotides opposite dG. Extension of primers from the termini opposite Î³-HOPdG was accomplished only following error-prone purine nucleotide incorporation. However, pol Î³ preferentially incorporated dT opposite the Î³-HOPdA adduct and efficiently extended primers from the correctly paired terminus, indicating that Î³-HOPdA is probably nonmutagenic. In summary, our data suggest that acrolein-induced exocyclic DNA lesions can be bypassed by mitochondrial DNA polymerase but, in the case of the minor groove Î³-HOPdG adduct, at the cost of unprecedented high mutation rates.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	20
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-05-17
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acrolein Pharmacology DNA Adducts DNA-Directed DNA Polymerase Metabolism Mitochondria Enzymology Catalytic Domain DNA Damage DNA Replication Deoxyguanosine Chemistry Lipid Peroxidation Models, Chemical Mutagenesis Oligonucleotides Oxidative Stress Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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