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Showing 1–13 of 13 results
Advanced filters: Author: Dmitry Temiakov Clear advanced filters

  • Mitochondrial DNA polymerases use different mechanisms for strand separation during replication. Here, the authors reveal the cryo-EM structures of yeast Mip1, identifying key structural elements that enable strand displacement. Mutations in these elements impair mitochondrial function and DNA maintenance.

    • Ashok R. Nayak
    • Viktoriia Sokolova
    • Dmitry Temiakov
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • Here, Herbine et al. use cryo-EM to establish how human mitochondrial polymerase performs substrate selection. The authors capture RNAP conformations representing the binding of a cognate nucleotide and the rejection of a non-cognate substrate.

    • Karl Herbine
    • Ashok R. Nayak
    • Dmitry Temiakov
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-9

  • Here, the authors use cryo-EM to capture nine intermediates along the DNA proofreading pathway using human mitochondrial DNA Polymerase Gamma. The results provide a step-by-step view of the DNA proofreading at single-nucleotide resolution.

    • Gina Buchel
    • Ashok R. Nayak
    • Dmitry Temiakov
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • The mitochondrial transcription factor A is excluded from the mitochondria in spermatozoa by virtue of phosphorylation of the mitochondrial presequence. This is associated with transport to the nucleus and loss of mitochondrial DNA (mtDNA) from the mitochondria, providing a mechanistic basis for uniparental inheritance of mtDNA in humans.

    • William Lee
    • Angelica Zamudio-Ochoa
    • Dmitry Temiakov
    Research
    Nature Genetics
    Volume: 55, P: 1632-1639

  • Mitochondrial DNA is transcribed by a single-subunit RNA polymerase (mtRNAP) that is distantly related to the RNAP of bacteriophage T7. Together with biochemical data, the crystal structure of the mtRNAP elongation complex with DNA template and RNA transcript elucidates the elongation mechanism of mtRNAP and reveals striking differences as compared with the T7 transcription system.

    • Kathrin Schwinghammer
    • Alan C M Cheung
    • Patrick Cramer
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1298-1303

  • Analysis of mitochondrial replacement therapy shows, even with efficient mutant mitochondrial DNA replacement and maintenance in embryonic stem cells, a gradual loss of donor mitochondrial DNA in some lines owing to a polymorphism in the D-loop, potentially causing preferential replication of specific mitochondrial DNA haplotypes.

    • Eunju Kang
    • Jun Wu
    • Shoukhrat Mitalipov
    Research
    Nature
    Volume: 540, P: 270-275

  • Cramer and colleagues review and discuss how the structural elucidation of transcription factors and functional complexes of human mitochondrial RNA polymerase have informed emerging understanding of the mechanism of mitochondrial gene transcription.

    • Hauke S. Hillen
    • Dmitry Temiakov
    • Patrick Cramer
    Reviews
    Nature Structural & Molecular Biology
    Volume: 25, P: 754-765