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Yeast DNA ligase IV mediates non-homologous DNA end joining

Author

Listed:
  • Thomas E. Wilson

    (Washington University School of Medicine
    Department of Pathology)

  • Ulf Grawunder

    (Department of Pathology
    University of Southern California)

  • Michael R. Lieber

    (Department of Pathology
    University of Southern California)

Abstract

The discovery of homologues from the yeast Saccharomyces cerevisiae of the human Ku DNA-end-binding proteins (HDF1 and KU80) has established that this organism is capable of non-homologous double-strand end joining (NHEJ)1,2,3,4,5, a form of DNA double-strand break repair (DSBR) active in mammalian V(D)J recombination6,7,8. Identification of the DNA ligase that mediates NHEJ in yeast will help elucidate the function of the four mammalian DNA ligases in DSBR, V(D)J recombination and other reactions9,10. Here we show that S. cerevisiae has two typical DNA ligases, the known DNA ligase I homologue CDC9 (refs 11,12, 13, 14) and the previously unknown DNA ligase IV homologue DNL4. dnl4 mutants are deficient in precise and end-processed NHEJ. DNL4 and HDF1 are epistatic in this regard, with the mutation of each having equivalent effects. dn14 mutants are complemented by overexpression of Dnl4 but not of Cdc9, and deficiency of Dnl4 alone does not impair either cell growth or the Cdc9-mediated responses to ionizing and ultraviolet radiation. Thus, S.cerevisiae has two distinct and separate ligation pathways.

Suggested Citation

  • Thomas E. Wilson & Ulf Grawunder & Michael R. Lieber, 1997. "Yeast DNA ligase IV mediates non-homologous DNA end joining," Nature, Nature, vol. 388(6641), pages 495-498, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6641:d:10.1038_41365
    DOI: 10.1038/41365
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