9D2I

Cryo-EM structure of the Strand displacement Complex (III) of Yeast Mitochondrial DNA polymerase Gamma (MIP1) with downstream DNA

9D2I の概要

• エントリーDOI: 10.2210/pdb9d2i/pdb
• 関連するPDBエントリー: 9C51 9C52 9C53
• EMDBエントリー: 46497
• 分子名称: DNA polymerase gamma, Primer DNA, Template DNA, ... (7 entities in total)
• 機能のキーワード: mitochondrial dna polymerase gamma, strand displacement complex, mip1, replication, helicase independent dna polymerase, transferase-dna complex
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 169672.52

構造登録者

Nayak, A.R.,Sokolova, V.O.,Sillamaa, S.,Sedmen, J.,Temiakov, D. (登録日: 2024-08-08, 公開日: 2025-03-19, 最終更新日: 2025-03-26)

主引用文献

Nayak, A.R.,Sokolova, V.,Sillamaa, S.,Herbine, K.,Sedman, J.,Temiakov, D.
Structural basis for intrinsic strand displacement activity of mitochondrial DNA polymerase.
Nat Commun, 16:2417-2417, 2025

PubMed Abstract: Members of the Pol A family of DNA polymerases, found across all domains of life, utilize various strategies for DNA strand separation during replication. In higher eukaryotes, mitochondrial DNA polymerase γ relies on the replicative helicase TWINKLE, whereas the yeast ortholog, Mip1, can unwind DNA independently. Using Mip1 as a model, we present a series of high-resolution cryo-EM structures that capture the process of DNA strand displacement. Our data reveal previously unidentified structural elements that facilitate the unwinding of the downstream DNA duplex. Yeast cells harboring Mip1 variants defective in strand displacement exhibit impaired oxidative phosphorylation and loss of mtDNA, corroborating the structural observations. This study provides a molecular basis for the intrinsic strand displacement activity of Mip1 and illuminates the distinct unwinding mechanisms utilized by Pol A family DNA polymerases.

PubMed: 40069189
DOI: 10.1038/s41467-025-57594-z

実験手法

ELECTRON MICROSCOPY (2.96 Å)