A single amino acid change in SNM1-encoded protein leads to thermoconditional deficiency for DNA cross-link repair in Saccharomyces cerevisiae.
Molecular characterization of a thermoconditional mutant snm1-2ts shows that the coding sequence contains three mutations, two of which are silent. The third changes amino acid glycine to arginine at position 256 thereby altering a hydrophilic domain of the protein. While sensitivity to nitrogen mustard of the mutant at 36 degrees C is very similar to that of the non-leaky allele snm1-1, multi-copy vector-mediated overexpression of snm1-2ts leads to a significantly reduced sensitivity to nitrogen mustard.
Niegemann
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E
Institut für Mikrobiologie, Abteilung Biologie für Mediziner, Frankfurt/Main, Germany.
Brendel
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M
D000595:Amino Acid Sequence; D001483:Base Sequence; D004260:DNA Repair / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000502:physiology; D004706:Endodeoxyribonucleases; D005656:Fungal Proteins / Q000235:genetics* / Q000502:physiology; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal / Q000235:genetics*; D005816:Genetic Complementation Test; D008466:Mechlorethamine / Q000494:pharmacology; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D016366:Open Reading Frames / Q000235:genetics; D017354:Point Mutation / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D013696:Temperature
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D008466:Mechlorethamine; D004706:Endodeoxyribonucleases; C090162:PSO2 protein, S cerevisiae