Molecular cloning of Drosophila mus308, a gene involved in DNA cross- link repair with homology to prokaryotic DNA polymerase I genes

Paul V. Harris, Olga M. Mazina, Edith A. Leonhardt, Ryan B. Case, James B. Boyd, Kenneth C. Burtis

Research output: Contribution to journalArticle

92 Scopus citations

Abstract

Mutations in the Drosophila mus308 gene confer specific hypersensitivity to DNA-cross-linking agents as a consequence of defects in DNA repair. The mus308 gene is shown here to encode a 229-kDa protein in which the amino- terminal domain contains the seven conserved motifs characteristic of DNA and RNA helicases and the carboxy-terminal domain shares over 55% sequence similarity with the polymerase domains of prokaryotic DNA polymerase I-like enzymes. This is the first reported member of this family of DNA polymerases in a eukaryotic organism, as well as the first example of a single polypeptide with homology to both DNA polymerase and helicase motifs. Identification of a closely related gene in the genome of Caenorhabditis elegans suggests that this novel polypeptide may play an evolutionarily conserved role in the repair of DNA damage in eukaryotic organisms.

Original languageEnglish (US)
Pages (from-to)5764-5771
Number of pages8
JournalMolecular and Cellular Biology
Volume16
Issue number10
StatePublished - 1996

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ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Harris, P. V., Mazina, O. M., Leonhardt, E. A., Case, R. B., Boyd, J. B., & Burtis, K. C. (1996). Molecular cloning of Drosophila mus308, a gene involved in DNA cross- link repair with homology to prokaryotic DNA polymerase I genes. Molecular and Cellular Biology, 16(10), 5764-5771.