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Mitochondrion. 2013 Nov;13(6):592-601. doi: 10.1016/j.mito.2013.08.003. Epub 2013 Aug 30.

Exonuclease of human DNA polymerase gamma disengages its strand displacement function.

Author information

1
Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.

Abstract

Pol γ, the only DNA polymerase found in human mitochondria, functions in both mtDNA repair and replication. During mtDNA base-excision repair, gaps are created after damaged base excision. Here we show that Pol γ efficiently gap-fills except when the gap is only a single nucleotide. Although wild-type Pol γ has very limited ability for strand displacement DNA synthesis, exo(-) (3'-5' exonuclease-deficient) Pol γ has significantly high activity and rapidly unwinds downstream DNA, synthesizing DNA at a rate comparable to that of the wild-type enzyme on a primer-template. The catalytic subunit Pol γA alone, even when exo(-), is unable to synthesize by strand displacement, making this the only known reaction of Pol γ holoenzyme that has an absolute requirement for the accessory subunit Pol γB.

KEYWORDS:

DNA repair and replication; Molecular motor; Strand displacement

PMID:
23993955
PMCID:
PMC5017585
DOI:
10.1016/j.mito.2013.08.003
[Indexed for MEDLINE]
Free PMC Article
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