title: Characterization of DNA polymerase beta mutants with amino acid substitutions located in the C-terminal portion of the enzyme.
abstract: We used quantitative complementation assays to characterize individual DNA polymerase beta (Pol beta) mutants for their ability to function in DNA replication and DNA repair. We also describe a screen for detecting mutator activity of DNA polymerase beta mutants. By using these bioassays, together with DNA polymerase activity gels, we characterized 15 new DNA polymerase beta mutants that display a wide spectrum of phenotypes. Most of these mutants are generally defective in their ability to synthesize DNA. However, two of our Pol beta mutants show more complex phenotypes: they are able to function in DNA repair but unable to participate in DNA replication. One of our mutants displays mutator activity in vivo. Our work provides a model to study mutant mammalian enzymes in Escherichia coli with phenotypes that are otherwise difficult to assess.
authors.affiliation: Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06510, USA.
authors.forename: J B
authors.initials: JB
authors.lastname: Sweasy
authors.forename: M S
authors.initials: MS
authors.lastname: Yoon
mesh_terms: D000818:Animals; D015153:Blotting, Western; D004256:DNA Polymerase I / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D004260:DNA Repair; D004261:DNA Replication; D004926:Escherichia coli / Q000235:genetics; D005816:Genetic Complementation Test; D008741:Methyl Methanesulfonate / Q000494:pharmacology; D016296:Mutagenesis; D009154:Mutation; D009608:Nitrous Acid / Q000494:pharmacology; D010641:Phenotype; D051381:Rats
chemical_list: D008741:Methyl Methanesulfonate; D004256:DNA Polymerase I; D009608:Nitrous Acid