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Research Article

Molecular Cloning of Drosophila mus308, a Gene Involved in DNA Cross-Link Repair with Homology to Prokaryotic DNA Polymerase I Genes†

, , , , &
Pages 5764-5771 | Received 26 Apr 1996, Accepted 01 Jul 1996, Published online: 29 Mar 2023
 

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.

Notes

† Dedicated to the memory of James B. Boyd.

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