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Nucleic Acids Research 2005 33(16):5094-5105; doi:10.1093/nar/gki813
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Published online 20 September 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

8-Oxoguanine incorporation into DNA repeats in vitro and mismatch recognition by MutS{alpha}

Peter Macpherson, Flavia Barone1, Giovanni Maga2, Filomena Mazzei1, Peter Karran and Margherita Bignami1,*

Cancer Research UK London Research Institute, Clare Hall Laboratories South Mimms, Herts, EN6 3LD, UK 1Department of Environment and Primary Prevention, Istituto Superiore di Sanita' Viale Regina Elena 299, 00161 Roma, Italy 2Istituto di Genetica Molecolare, IGM-CNR, National Research Council Via Abbiategrasso 207, 27100 Pavia, Italy

*To whom correspondence should be addressed. Tel: +39 06 49902355; Fax: +39 06 49903650; Email: bignami{at}iss.it

Received June 28, 2005. Revised July 28, 2005. Accepted August 17, 2005.

DNA 8-oxoguanine (8-oxoG) causes transversions and is also implicated in frameshifts. We previously identified the dNTP pool as a likely source of mutagenic DNA 8-oxoG and demonstrated that DNA mismatch repair prevented oxidation-related frameshifts in mononucleotide repeats. Here, we show that both Klenow fragment and DNA polymerase {alpha} can utilize 8-oxodGTP and incorporate the oxidized purine into model frameshift targets. Both polymerases incorporated 8-oxodGMP opposite C and A in repetitive DNA sequences and efficiently extended a terminal 8-oxoG. The human MutS{alpha} mismatch repair factor recognized DNA 8-oxoG efficiently in some contexts that resembled frameshift intermediates in the same C or A repeats. DNA 8-oxoG in other slipped/mispaired structures in the same repeats adopted configurations that prevented recognition by MutS{alpha} and by the OGG1 DNA glycosylase thereby rendering it invisible to DNA repair. These findings are consistent with a contribution of oxidative DNA damage to frameshifts. They also suggest how mismatch repair might reduce the burden of DNA 8-oxoG and prevent frameshift formation.


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