Abstract:
:Mitochondrial aprataxin (APTX) protects the mitochondrial genome from the consequence of ligase failure by removing the abortive ligation product, i.e. the 5'-adenylate (5'-AMP) group, during DNA replication and repair. In the absence of APTX activity, blocked base excision repair (BER) intermediates containing the 5'-AMP or 5'-adenylated-deoxyribose phosphate (5'-AMP-dRP) lesions may accumulate. In the current study, we examined DNA polymerase (pol) γ and pol β as possible complementing enzymes in the case of APTX deficiency. The activities of pol β lyase and FEN1 nucleotide excision were able to remove the 5'-AMP-dRP group in mitochondrial extracts from APTX-/- cells. However, the lyase activity of purified pol γ was weak against the 5'-AMP-dRP block in a model BER substrate, and this activity was not able to complement APTX deficiency in mitochondrial extracts from APTX-/-Pol β-/- cells. FEN1 also failed to provide excision of the 5'-adenylated BER intermediate in mitochondrial extracts. These results illustrate the potential role of pol β in complementing APTX deficiency in mitochondria.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Çaglayan M,Prasad R,Krasich R,Longley MJ,Kadoda K,Tsuda M,Sasanuma H,Takeda S,Tano K,Copeland WC,Wilson SHdoi
10.1093/nar/gkx654subject
Has Abstractpub_date
2017-09-29 00:00:00pages
10079-10088issue
17eissn
0305-1048issn
1362-4962pii
4037357journal_volume
45pub_type
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