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Crucial role for DNA ligase III in mitochondria but not in Xrcc1-dependent repair

Author

Listed:
  • Deniz Simsek

    (Developmental Biology Program, Memorial Sloan-Kettering Cancer Center
    Weill Cornell Graduate School of Medical Sciences)

  • Amy Furda

    (University of Pittsburgh School of Medicine and The University of Pittsburgh Cancer Institute, Hillman Cancer Center)

  • Yankun Gao

    (St Jude Children’s Research Hospital)

  • Jérôme Artus

    (Developmental Biology Program, Memorial Sloan-Kettering Cancer Center)

  • Erika Brunet

    (Developmental Biology Program, Memorial Sloan-Kettering Cancer Center
    Museum National d’Histoire Naturelle, 43 rue Cuvier
    CNRS, UMR7196, 43 rue Cuvier
    Inserm, U565, 43 rue Cuvier)

  • Anna-Katerina Hadjantonakis

    (Developmental Biology Program, Memorial Sloan-Kettering Cancer Center
    Weill Cornell Graduate School of Medical Sciences)

  • Bennett Van Houten

    (University of Pittsburgh School of Medicine and The University of Pittsburgh Cancer Institute, Hillman Cancer Center)

  • Stewart Shuman

    (Weill Cornell Graduate School of Medical Sciences
    Molecular Biology Program, Memorial Sloan-Kettering Cancer Center)

  • Peter J. McKinnon

    (St Jude Children’s Research Hospital)

  • Maria Jasin

    (Developmental Biology Program, Memorial Sloan-Kettering Cancer Center
    Weill Cornell Graduate School of Medical Sciences)

Abstract

A mitochondrial role for DNA ligase III Mammalian cells contain three different DNA ligase enzymes, each with different properties but all involved in DNA replication and repair. Ligase III (Lig3) is known to form a complex with the nuclear DNA repair protein Xrcc1, and Lig3 null animals cannot be made. This raises the question of whether this nuclear role in base-excision repair (BER) is the critical function of Lig3 that maintains viability. Two groups reporting in this issue of Nature investigate different aspects of Lig3 function in vivo, both concluding that the catalytic activity of Lig3 is critical for mitochondrial DNA maintenance and viability, but unexpectedly, is dispensable for Xrcc1-mediated nuclear BER. These findings suggest that Lig3 mutations might cause some of the human syndromes associated with defects in the replication and/or repair of mitochondrial DNA.

Suggested Citation

  • Deniz Simsek & Amy Furda & Yankun Gao & Jérôme Artus & Erika Brunet & Anna-Katerina Hadjantonakis & Bennett Van Houten & Stewart Shuman & Peter J. McKinnon & Maria Jasin, 2011. "Crucial role for DNA ligase III in mitochondria but not in Xrcc1-dependent repair," Nature, Nature, vol. 471(7337), pages 245-248, March.
    • Handle: RePEc:nat:nature:v:471:y:2011:i:7337:d:10.1038_nature09794
    DOI: 10.1038/nature09794
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    Cited by:

    1. Sandra Wimberger & Nina Akrap & Mike Firth & Johan Brengdahl & Susanna Engberg & Marie K. Schwinn & Michael R. Slater & Anders Lundin & Pei-Pei Hsieh & Songyuan Li & Silvia Cerboni & Jonathan Sumner &, 2023. "Simultaneous inhibition of DNA-PK and Polϴ improves integration efficiency and precision of genome editing," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Manohar Kodavati & Haibo Wang & Wenting Guo & Joy Mitra & Pavana M. Hegde & Vincent Provasek & Vikas H. Maloji Rao & Indira Vedula & Aijun Zhang & Sankar Mitra & Alan E. Tomkinson & Dale J. Hamilton &, 2024. "FUS unveiled in mitochondrial DNA repair and targeted ligase-1 expression rescues repair-defects in FUS-linked motor neuron disease," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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