ArticleNucleic acids research2026
Pol γ possesses separate metal binding sites for polymerase and strand displacement functions.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Molecular and structural basis for replication initiation and strand separation by human mitochondrial DNA polymerase γ.Nucleic acids research · 2026Article
- Structural Basis of Polypurine Track Strand Displacement by HIV-1 Reverse Transcriptase.bioRxiv : the preprint server for biology · 2026Article
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Abstract
Accurate replication of the mitochondrial genome (mtDNA) depends on DNA polymerase γ (Pol γ), yet its strand-displacement activity has been reported with varying outcomes across studies. Here we show that human Pol γ carries out robust, processive strand-displacement synthesis under physiological divalent metal-ion concentrations. We identify two functional classes of metal-binding sites: high-affinity sites that support DNA synthesis and unwinding, and low-affinity sites that selectively suppress unwinding without impairing polymerase activity. Pol γ efficiently displaces DNA/DNA duplex and RNA/DNA hybrids, supporting a role in RNA primer removal during mtDNA replication. Cryo-EM structures of Pol γ bound to fork-mimicking DNA reveal conformational states corresponding to progressive duplex unwinding and identify structural elements that facilitate strand displacement. These findings establish a metal-dependent mechanism for Pol γ activity and reconcile previous discrepancies in its reported unwinding capacity.
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