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Nucleic Acids Research 2005 33(12):3722-3732; doi:10.1093/nar/gki683
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Published online 8 July 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}oupjournals.org

Article

Localization of mitochondrial DNA base excision repair to an inner membrane-associated particulate fraction

J. A. Stuart, S. Mayard, K. Hashiguchi, N. C. Souza-Pinto and V. A. Bohr*

Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health 5600 Nathan Shock Drive, Box 1, Baltimore, MD 21224, USA

*To whom correspondence should be addressed. Tel: +1 410 558 8332; Fax: +1 410 558 8157; Email: bohrv{at}grc.nia.nih.gov

Received March 24, 2005. Revised June 13, 2005. Accepted June 13, 2005.

Mitochondrial DNA (mtDNA) contains high levels of oxidative damage relative to nuclear DNA. A full, functional DNA base excision repair (BER) pathway is present in mitochondria, to repair oxidative DNA lesions. However, little is known about the organization of this pathway within mitochondria. Here, we provide evidence that the mitochondrial BER proteins are not freely soluble, but strongly associated with an inner membrane-containing particulate fraction. Uracil DNA glycosylase, oxoguanine DNA glycosylase and DNA polymerase {gamma} activities all co-sedimented with this particulate fraction and were not dissociated from it by detergent (0.1% or 1.0% NP40) treatment. The particulate associations of these activities were not due to their binding mtDNA, which is itself associated with the inner membrane, as they also localized to the particulate fraction of mitochondria from 143B (TK–) {rho}0 cells, which lack mtDNA. However, all of the BER activities were at least partially solubilized from the particulate fraction by treatment with 150–300 mM NaCl, suggesting that electrostatic interactions are involved in the association. The biological implications of the apparent immobilization of BER proteins are discussed.

Present address: J. A. Stuart, Department of Biology, Brock University, St Catharines, Ontario, Canada L2S 3A1


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