ArticlePloS one2012
C-terminal extension of the yeast mitochondrial DNA polymerase determines the balance between synthesis and degradation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Structural basis for intrinsic strand displacement activity of mitochondrial DNA polymerase.Nature communications · 2025Article
- PCNA and Rnh1 independently participate in the protection of mitochondrial genome against UV-induced mutagenesis in yeast cells.Scientific reports · 2024Article
- Regulation with cell size ensures mitochondrial DNA homeostasis during cell growth.Nature structural & molecular biology · 2023Article
- Bst polymerase - a humble relative of Taq polymerase.Computational and structural biotechnology journal · 2023Review
- Review
- A non-radioactive DNA synthesis assay demonstrates that elements of the Sigma 1278b Mip1 mitochondrial DNA polymerase domain and C-terminal extension facilitate robust enzyme activity.Yeast (Chichester, England) · 2021Article
- Yeast model analysis of novel polymerase gamma variants found in patients with autosomal recessive mitochondrial disease.Human genetics · 2015Article
- DNA polymerase γ and disease: what we have learned from yeast.Frontiers in genetics · 2015Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae mitochondrial DNA polymerase (Mip1) contains a C-terminal extension (CTE) of 279 amino acid residues. The CTE is required for mitochondrial DNA maintenance in yeast but is absent in higher eukaryotes. Here we use recombinant Mip1 C-terminal deletion mutants to investigate functional importance of the CTE. We show that partial removal of the CTE in Mip1Δ216 results in strong preference for exonucleolytic degradation rather than DNA polymerization. This disbalance in exonuclease and polymerase activities is prominent at suboptimal dNTP concentrations and in the absence of correctly pairing nucleotide. Mip1Δ216 also displays reduced ability to synthesize DNA through double-stranded regions. Full removal of the CTE in Mip1Δ279 results in complete loss of Mip1 polymerase activity, however the mutant retains its exonuclease activity. These results allow us to propose that CTE functions as a part of Mip1 polymerase domain that stabilizes the substrate primer end at the polymerase active site, and is therefore required for efficient mitochondrial DNA replication in vivo.
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