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  • Mutagen hyper-resistance  (3)
  • Alcohol dehydrogenase  (2)
  • Interstrand cross-links  (2)
  • 1
    Electronic Resource
    Electronic Resource
    The SNQ3 gene of Saccharomyces cerevisiae confers hyper-resistance to several functionally unrelated chemicals (1991)
    Springer
    Current genetics 19 (1991), S. 429-433 
    Details
    ISSN: 1432-0983
    Keywords: Mutagen hyper-resistance ; Yeast ; Base sequence ; Gene disruption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A multi-copy plasmid containing the SNQ3 gene confers hyper-resistance to 4-nitroquinoline-N-oxide (4NQO), Trenimon, MNNG, cycloheximide, and to sulfometuron methyl in yeast transformants. Restriction analysis, subcloning, and DNA sequencing revealed an open reading frame of 1950 bp on the SNQ3-containing insert DNA. Gene disruption and transplacement into chromosomal DNA yielded 4NQO-sensitive null mutants which were also more sensitive than the wild-type to Trenimon, cycloheximide, sulfometuron methyl, and MNNG. Hydropathic analysis showed that the SNQ3-encoded protein is most likely not membrane-bound, while the codon bias index points to low expression of the gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00312733
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  • 2
    Electronic Resource
    Electronic Resource
    Formation and stability of interstrand cross-links induced by cis- and trans-diamminedichloroplatinum (II) in the DNA of Saccharomyces cerevisiae strains differing in repair capacity (1989)
    Springer
    Current genetics 16 (1989), S. 331-338 
    Details
    ISSN: 1432-0983
    Keywords: Platinum compounds ; Yeast ; Repair mutants ; Interstrand cross-links ; DNA degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Four haploid yeast strains differing in proficiency for DNA repair were treated with cis- or transDDP. The wild type was least sensitive while the excision-deficient mutants rad1, rad2 and snm1exhibited higher sensitivities to either platinum compound. In all four strains tested cisDDP showed a two- to five-fold higher cytotoxicity than equimolar concentrations of transDDP. DNA interstrand cross-linking was caused by both agents in all strains. However, transDDP introduced more DNA cross-links at exposure times up to 6 h while cisDDP was the more active cross-linking agent at longer times. There was no clear-cut correlation of the number of DNA interstrand cross-links with survival. Formaldehyde-treated cells showed DNA with lower buoyant density due to proteinase K sensitive DNA-protein cross-linking; this effect was not observed after treatment with either platinum compound. Post-treatment incubation of wild-type cells exposed to cisDDP led to degradation of DNA by single and double-strand breaks, parallel with further increase of DNA interstrand cross-linking. DNA from transDDP-treated cells did not show extensive degradation although interstrand cross-links were lost during liquid holding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00340711
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  • 3
    Electronic Resource
    Electronic Resource
    A recessive mutant allele of the HNM1 gene of Saccharomyces cerevisiae is responsible for hyper-resistance to nitrogen mustard (1990)
    Springer
    Current genetics 18 (1990), S. 187-192 
    Details
    ISSN: 1432-0983
    Keywords: Mutagen hyper-resistance ; Nitrogen mustard ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A screening of haploid yeast strains for enhanced resistance to nitrogen mustard (HN2) yielded a recessive mutant allele, hnm1, that conferred hyper-resistance (HYR) to HN2. Diploids, homo- or heterozygous for the HNM1 locus, exhibit normal wild-type like resistance while homozygosity for hnm1 leads to the phenotype HYR to HN2. The hnm1 mutation could be found in yeast strains proficient or deficient in different DNA repair systems. In these mostly HN2-sensitive haploid repair-deficient mutants, hnm1 acted as a partial suppressor of HN2 sensitivity. All isolated recessive mutations conferring hyper-resistance belonged to a single complementations group. The HYR to HN2 phenotype was maximally expressed in growing cells and was associated with reduced mutability by HN2. HNM1 most probably controls uptake of HN2 which would be impaired in the hnm1 mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318378
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  • 4
    Electronic Resource
    Electronic Resource
    Overexpression ofADH1 confers hyper-resistance to formaldehyde inSaccharomyces cerevisiae (1996)
    Springer
    Current genetics 29 (1996), S. 437-440 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Formaldehyde ; Hyper-resistance ; Alcohol dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In an attempt to clone genes involved in resistance to formaldehyde we have screened a genomic library based on the episomal plasmid YEp24 for the ability to increase resistance to formaldehyde in a wild-type strain. In addition toSFA, the gene encoding the formaldehyde dehydrogenase Adh5, an enzyme most potent in formaldehyde de-toxification, we isolated a second plasmid that conferred a less pronounced but significant hyper-resistance to formaldehyde. Its passenger DNA contained the geneADH1, encoding alcohol dehydrogenase 1 (EC 1.1.1.1), which could be shown to be responsible for the observed hyper-resistance phenotype. Construction of anadh1-0 mutant revealed that yeast lacking a functionalADH1 gene is sensitive to formaldehyde. While glutathione is essential for Adh5-mediated formaldehyde de-toxification, Adh1 reduced formaldehyde best in the absence of this thiol compound. Evidence is presented that formaldehyde is a substrate for Adh1 in vivo and in vitro and that its cellular de-toxification employs a reductive step that may yield methanol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02221511
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular structure of the DNA cross-link repair gene SNM1(PSO2) of the yeast Saccharomyces cerevisiae (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 194-200 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; DNA repair ; Nitrogen mustard ; Interstrand cross-links ; Nucleotide sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 3.2 kb yeast DNA fragment containing the DNA interstrand cross-link-specific repair gene SNM1 has been sequenced. Two genes were identified. SNM1 has an open reading frame of 1983 by and codes for a 661 amino acid protein. Hydrophobic analysis shows that the protein is most probably not directly membrane bound. The second gene, UGX1, has an open reading frame of 573 by coding for a polypeptide of 191 amino acid residues. The two genes are arranged head to head and share a 192 by divergent promoter region that contains three TATAAA motives, two for the SNM1 and one for the UGX1 locus. Gene UGX1 has no apparent influence on the sensitivity of the cell to cross-linking nitrogen mustard, as its disruption in wild type does not increase sensitivity to nitrogen mustard and the presence of multiple copies of the gene fails to complement the nitrogen mustard sensitivity phenotype of snm1 disruption mutants. Northern analysis revealed that the expression of SNM1 yields an average of 0.3 copies/cell of a 2.4 kb transcript, while expression of UGX1 yields higher levels of a 0.8 kb poly(A)+ RNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00279791
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  • 6
    Electronic Resource
    Electronic Resource
    Gene SNQ2 of Saccharomyces cerevislae, which confers resistance to 4-nitroquinoline-N-oxide and other chemicals, encodes a 169 kDa protein homologous to ATP-dependent permeases (1993)
    Springer
    Molecular genetics and genomics 236 (1993), S. 214-218 
    Details
    ISSN: 1617-4623
    Keywords: Mutagen hyper-resistance ; 4-nitroquinolineN-oxide ; Yeast ; ATP-dependent permease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The yeast gene SNQ2 confers hyper-resistance to the mutagens 4-nitroquinoline-N-oxide (4-NQO) and Triaziquone, as well as to the chemicals sulphomethuron methyl and phenanthroline when present in multiple copies in transformants of Saccharomyces cerevisiae. Subcloning and sequencing of a 5.5 kb yeast DNA fragment revealed that SNQ2 has an open reading frame of 4.5 kb. The putative encoded polypeptide of 1501 amino acids has a predicted molecular weight of 169 kDa and has several hydrophobic regions. Northern analysis showed a transcript of 5.5 kb. Haploid cells with a disrupted SNQ2 reading frame are viable. The SNQ2-encoded protein has domains believed to be involved in ATP binding and is likely to be membrane associated. It most probably serves as an ATP-dependent permease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00277115
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  • 7
    Electronic Resource
    Electronic Resource
    Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its protein product (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 351-358 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Formaldehyde hyper-resistance ; Alcohol dehydrogenase ; Glutathione ; Inducibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 3.7 kb DNA fragment of yeast chromosome IV has been sequenced that contains the SFA gene which, when present on a multi-copy plasmid in Saccharomyces cerevisiae, confers hyper-resistance to formaldehyde. The open reading frame of SFA is 1158 by in size and encodes a polypeptide of 386 amino acids. The predicted protein shows strong homologies to several mammalian alcohol dehydrogenases and contains a sequence characteristic of binding sites for NAD. Overexpression of the SFA gene leads to enhanced consumption of formaldehyde, which is most probably the reason for the observed hyper-resistance phenotype. In sfa:LEU2 disruption mutants, sensitivity to formaldehyde is correlated with reduced degradation of the chemical. The SFA gene shares an 868 by divergent promoter with UGX2 a gene of yet unknown function. Promoter deletion studies with a SFA promoter-lacZ gene fusion construct revealed negative interference on expression of SFA by upstream sequences. The upstream region between positons − 145 and − 172 is totally or partially responsible for control of inducibility of SFA by chemicals such as formaldehyde (FA), ethanol and methyl methanesulphonate. The 41 kDa SFA-encoded protein was purified from a hyper-resistant transformant; it oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize FA. SFA is predicted to code for a long-chain alcohol dehydrogenase (glutathione-dependent formaldehyde dehydrogenase) of the yeast S. cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00279438
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