論文

査読有り
2005年

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

NUCLEIC ACIDS RESEARCH
  • JA Stuart
  • ,
  • S Mayard
  • ,
  • K Hashiguchi
  • ,
  • NC Souza-Pinto
  • ,
  • VA Bohr

33
12
開始ページ
3722
終了ページ
3732
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/gki683
出版者・発行元
OXFORD UNIV PRESS

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.

リンク情報
DOI
https://doi.org/10.1093/gki683
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/16006620
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000230725400010&DestApp=WOS_CPL
ID情報
  • DOI : 10.1093/gki683
  • ISSN : 0305-1048
  • PubMed ID : 16006620
  • Web of Science ID : WOS:000230725400010

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