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  • Saccharomyces cerevisiae  (412)
  • Yeast  (350)
  • Springer  (732)
  • American Institute of Physics
  • American Institute of Physics (AIP)
  • 2005-2009
  • 1990-1994  (419)
  • 1985-1989  (313)
  • 1950-1954
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  • 1
    Electronic Resource
    Electronic Resource
    Adaptation of a Saccharomyces cerevisiae strain to high copper concentrations (1994)
    Springer
    BioMetals 7 (1994), S. 221-226 
    Details
    ISSN: 1572-8773
    Keywords: catalase ; copper resistance ; pH-dependent growth ; Saccharomyces cerevisiae ; superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A strain of Saccharomyces cerevisiae has been adapted to increasing concentrations of copper at two different pH values. The growth curve at pH 5.5 is characterized by a time generation increasing with the amount of added copper. A significant decrease of cell volume as compared with the control is also observed. At pH 3 the cells grow faster than at pH 5.5 and resist higher copper concentrations (3.8 against 1.2 mm). Experimental evidence indicates that, after copper treatment, the metal is not bound to the cell wall, but is localized intracellularly. A significant precipitation of copper salts in the medium was observed only at pH 5.5. Increased levels of superoxide dismutase (SOD) activity were observed in copper-treated cells and which persisted after 20 subsequent inocula in a medium without added metal. On the contrary, catalase activity was not stimulated by copper treatment and, hence, not correlated with SOD levels. The mechanism of copper resistance, therefore, probably involves a persistent induction of SOD, but not of catalase, and it is strongly pH-dependent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00149552
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular evolution of the HSP70 multigene family (1994)
    Springer
    Journal of molecular evolution 38 (1994), S. 1-17 
    Details
    ISSN: 1432-1432
    Keywords: HSP70 ; Heat shock ; Evolution ; Phylogeny ; Yeast ; Multigene family ; Subcellular compartmentalization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Eukaryotic genomes encode multiple 70-kDa heat-shock proteins (HSP70s). The Saccharomyces cerevisiae HSP70 family is comprised of eight members. Here we present the nucleotide sequence of the SSA3 and SSB2 genes, completing the nucleotide sequence data for the yeast HSP70 family. We have analyzed these yeast sequences as well as 29 HSP70s from 24 additional eukaryotic and prokaryotic species. Comparison of the sequences demonstrates the extreme conservation of HSP70s; proteins from the most distantly related species share at least 45% identity and more than one-sixth of the amino acids are identical in the aligned region (567 amino acids) among all proteins analyzed. Phylogenetic trees constructed by two independent methods indicate that ancient molecular and cellular events have given rise to at least four monophyletic groups of eukaryotic HSP70 proteins. Each group of evolutionarily similar HSP70s shares a common intracellular localization and is presumed to be comprised of functional homologues; these include heat-shock proteins of the cytoplasm, endoplasmic reticulum, mitochondria, and chloroplasts. HSP70s localized in mitochondria and plastids are most similar to the DnaK HSP70 homologues in purple bacteria and cyanobacteria, respectively, which is consistent with the proposed prokaryotic origin of these organelles. The analyses indicate that the major eukaryotic HSP70 groups arose prior to the divergence of the earliest eukaryotes, roughly 2 billion years ago. In some cases, as exemplified by the SSA genes encoding the cytoplasmic HSP70s of S. cerevisiae, more recent duplication events have given rise to subfamilies within the major groups. The S. cerevisiae SSB proteins comprise a unique subfamily not identified in other species to date. This subfamily appears to have resulted from an ancient gene duplication that occurred at approximately the same time as the origin of the major eukaryotic HSP70 groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00175490
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  • 3
    Electronic Resource
    Electronic Resource
    Chimeric evolution of the 2-μm genome in Saccharomyces cerevisiae (1994)
    Springer
    Journal of molecular evolution 38 (1994), S. 363-368 
    Details
    ISSN: 1432-1432
    Keywords: Saccharomyces cerevisiae ; 2-μm circle ; DNA sequencing ; Horizontal transmission ; Site-specific recombination ; Selfish DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We compared the nucleotide substitution pattern over the entire genome of two unique variants of the 6,300-bp selfish DNA (2 μm) plasmid in Saccharomyces cerevisiae. The DNA sequence of the left-unique region is identical among 2-μm variants, while the right-unique region shows substantial divergence. This chimeric pattern cannot be explained by neutral or Darwinian selection models. We propose that horizontal transmission of the 2-μm plasmid coupled with a directed, polarized gene conversion maintains the DNA sequence of the left-unique region, whereas the right-unique region is subject to random drift and Darwinian selection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00163153
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  • 4
    Electronic Resource
    Electronic Resource
    Mistranslation of human phosphoglycerate kinase in yeast in the presence of paromomycin (1994)
    Springer
    Current genetics 26 (1994), S. 95-99 
    Details
    ISSN: 1432-0983
    Keywords: Translational fidelity ; Paromomycin ; Stuttering ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Missense errors in the translation of mRNAs in Saccharomyces cerevisiae were screened by looking for charge heterogeneity of proteins on two-dimensional gels resulting from the substitution of charged and neutral amino acids. No such mistranslation was detected in wild-type yeast strains grown in the presence of the translational error-inducing antibiotic paromomycin. However, paromomycin-induced mistranslation of a heterologous mRNA, encoding human phosphoglycerate kinase expressed in yeast, was seen. We suggest that the combination of error-prone translation of a heterologous mRNA, and growth in the presence of paromomycin, leads to an accumulation of mistranslated proteins that can be detected by two-dimensional gel electrophoresis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313794
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  • 5
    Electronic Resource
    Electronic Resource
    Heat shock changes the response of the pso3 mutant of Saccharomyces cerevisiae to 8-methoxypsoralen photoaddition (1994)
    Springer
    Current genetics 26 (1994), S. 100-104 
    Details
    ISSN: 1432-0983
    Keywords: DNA repair ; Heat shock ; Hyperthermia ; Mutagenesis ; pso3-1 mutant ; Psoralen ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A putative tolerance, induced by heat shock (HS), to the lethal and mutagenic effects of 8-methoxypsoralen (8-MOP) photoaddition and hyperthermia was analyzed in Saccharomyces cerevisiae using the wild-type strain N123 and the isogenic DNA repair-deficient mutant pso3-1. In wild-type cells, the HS (38°C for 1 h) did not modify either the survival or the mutation frequency observed after 8-MOP photoaddition, even though it conferred protection against the lethal effect of hyperthermia (50°C). In the pso3-1 mutant, HS induced an increase of the survival, and a decrease of the mutation frequency, after 8-MOP photoaddition and it also protected against the lethal effect of hyperthermia. The responses induced by HS were specific for 8-MOP photoaddition, since they were not observed after 254 nm ultraviolet-light damage. These results indicate that the protection conferred by HS depends of the type of lesion, and operates through the induction of different repair processes. In the pso3-1 mutant, HS could channel the repair intermediates to and error-free repair pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313795
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  • 6
    Electronic Resource
    Electronic Resource
    Energy-dependent mitochondrial mutagenicity of antibacterial ofloxacin and its recombinogenic activity in yeast (1994)
    Springer
    Current genetics 26 (1994), S. 281-284 
    Details
    ISSN: 1432-0983
    Keywords: Ofloxacin ; Mitochondria ; Mutation ; Recombination ; Topoisomerase ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ofloxacin, a specific inhibitor of bacterial topoisomerase II, is known to inhibit the growth of yeast cells and to induce rho − mutants in the yeast S. cerevisiae. The frequency of ofloxacin-induced petite mutants under non-growth conditions was found to be strongly diminished when the cells were depleted in intramitochondrial ATP. Under optimal conditions of mitochondrial mutagenesis the drug induced mitotic recombination and reverse mutation in diploid strains but failed to cure either killer plasmids or the 2 μm DNA of dividing cells. The sensitivity to ofloxacin of the strains deficient in the DNA strandbreak repair pathway (rad52) was significantly higher then that of the wild-type strains and of the mutants deficient in excision or mutagenic DNA repair. The results are compatible with the idea that the cytotoxic and genetic activity of ofloxacin in yeast probably results from the inhibited DNA ligation function of topoisomerase II creating DNA breaks that are reparable through the recombination repair pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309561
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  • 7
    Electronic Resource
    Electronic Resource
    Saccharomyces cerevisiae YDR1, which encodes a member of the ATP-binding cassette (ABC) superfamily, is required for multidrug resistance (1994)
    Springer
    Current genetics 26 (1994), S. 285-294 
    Details
    ISSN: 1432-0983
    Keywords: ABC superfamily ; Multidrug resistance ; Saccharomyces cerevisiae ; YDR1 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A multidrug resistance gene, YDR1, of Saccharomyces cerevisiae, which encodes a 170-kDa protein of a member of the ABC superfamily, was identified. Disruption of YDR1 resulted in hypersensitivity to cycloheximide, cerulenin, compactin, staurosporine and fluphenazine, indicating that YDR1 is an important determinant of cross resistance to apparently-unrelated drugs. The Ydr1 protein bears the highest similarity to the S. cerevisiae Snq2 protein required for resistance to the mutagen 4-NQO. The drug-specificity analysis of YDR1 and SNQ2 by gene disruption, and its phenotypic suppression by the overexpressed genes, revealed overlapping, yet distinct, specificities. YDR1 was responsible for cycloheximide, cerulenin and compactin resistance, whereas, SNQ2 was responsible for 4-NQO resistance. The two genes had overlapping specificities toward staurosporine and fluphenazine. The transcription of YDR1 and SNQ2 was induced by various drugs, both relevant and irrelevant to the resistance caused by the gene, suggesting that drug specificity can be mainly attributed to the functional difference of the putative transporters. The transcription of these genes was also increased by heat shock. The yeast drug-resistance system provides a novel model for mammalian multidrug resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310491
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  • 8
    Electronic Resource
    Electronic Resource
    The byp1-3 allele of the Saccharomyces cerevisiae GGS1/TPS1 gene and its multi-copy suppressor tRNAGLN (CAG): Ggs1/Tps1 protein levels restraining growth on fermentable sugars and trehalose accumulation (1994)
    Springer
    Current genetics 26 (1994), S. 295-301 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Trehalose synthase ; GGS1/TPS1 gene ; Glycolysis ; Fermentable sugars ; Suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Byp1-3 is an amber nonsense allele of the Sacchromyces cerevisiae GGS1/TPS1 gene which encodes the small subunit of the trehalose synthase complex. Mutations in this gene confer an inability to grow on glucose or fructose but the phenotype of byp1-3 mutants is leaky in a strain-dependent manner. Overexpression of the isolated byp1-3 allele suppressed the growth defect of a ggs1/tps1Δ mutant. Expression of an in-vitro-generated mutant allele of GGS1/TPS1 that lacks all the coding sequences downstream from the byp1-3 mutation led to the production of a shortened protein that did not complement the ggs1/tps1Δ mutant. We have isolated, as an allele-specific multi-copy suppressor of the growth defect of the byp1-3 mutant on fructose, the gene for tRNAGLN (CAG). Thus the leaky phenotype of byp1-3 mutants is due to a low level of read through of the internal nonsense codon by tRNAGLN (CAG). Using overexpression of the isolated byp1-3 allele, as well as of the tRNAGLN (CAG) gene, we were able to demonstrate that as little as about 10% of the normal Ggs1/Tps1 protein level is sufficient for slow growth on fructose. We also show a correlation between the level of Ggs1/Tps1, the ability to accumulate trehalose in stationary phase and the ability to grow on fermentable sugars. Sequence analysis of the cloned tRNAGLN (CAG) gene showed that it is located 700 bp upstream of URA10. However, we found considerable differences to the reported sequence of URA10, in particular in the non-coding region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310492
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  • 9
    Electronic Resource
    Electronic Resource
    The yeast protein Mrs6p, a homologue of the rabGDI and human choroideraemia proteins, affects cytoplasmic and mitochondrial functions (1994)
    Springer
    Current genetics 26 (1994), S. 308-314 
    Details
    ISSN: 1432-0983
    Keywords: Small G proteins ; YPT1 ; Yeast ; abGDI ; Mitochondria ; MRS2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract MRS6 is a newly-identified gene in the yeast Saccharomyces cerevisiae. Its product Mrs6p shows significant homology to the mammalian GDP dissociation inhibitor (GDI) of Rab/Ypt-type small G proteins and to the human choroideraemia protein (CHM), the component A of Rab-specific GGTase II. The interaction of Mrs6p with G proteins is indicated by our observation that the MRS6 gene suppresses the effect of a temperature-sensitive ypt1 mutation. Disruption of the MRS6 gene is lethal to haploid yeast cells. This is consistent with the notion that Mrs6p is interacting with Rab/Ypt-type small G proteins, which are known to have essential functions in vesicular transport. Unexpeciedly, the MRS6 gene product also affects mitochondrial functions as revealed by the facts that highcopy numbers of MRS6 (1) suppress the pet - phenotype of mrs2-1 mutant strains and (2) cause a weak pet - phenotype in wild-type strains. We conclude from these results that the MRS6 gene product has a vital function in connection with Rab/Ypt-type proteins in the cytoplasm and, in addition, affects mitochondrial functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310494
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  • 10
    Electronic Resource
    Electronic Resource
    LYC1 is the structural gene for lysine N-6-acetyl transferase in yeast (1994)
    Springer
    Current genetics 25 (1994), S. 24-29 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Yarrowia lipolytica ; Lysine acetyl transferase ; Lysine catabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the yeastYarrowia lipolytica, theLYC1 locus controls the first step of the lysine degradation pathway which is catalyzed by lysine N-6-acetyl transferase (LAT). This gene was cloned by complementation of thelyc1-100 mutation. Its position in the cloned insert was determined by conversion mapping and by complementation. TheLYC1 gene encodes a 391 amino-acid polypeptide which has no homolog in protein databases. The required upstream region extends over 960 bp. When placed under the control of theGAL10 promoter inSaccharomyces cerevisiae, LYC1 drives the expression of lysine acetyl transferase activity, thus providing strong evidence that it is the structural gene encoding this enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712962
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  • 11
    Electronic Resource
    Electronic Resource
    Genetic effects of photoactivated psoralens during meiosis in DNA repair mutantpso3-1 ofSaccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 19-23 
    Details
    ISSN: 1432-0983
    Keywords: Psoralen ; DNA repair mutants ; Gene conversion ; Recombination ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The influence of the DNA repair genePSO3 on photoactivated psoralen-induced meiotic recombination, gene conversion, reverse mutation, and on survival, was assayed in diploid strains ofSaccharomyces cerevisiae homozygous for the wild-type or thepso3-1 mutant allele. Sporulation was normal in thepso3-1 diploid. Wild-type and mutant strains had the same sensitivity to photoactivated monofunctional psoralen (3-CPs+UVA) in meiosis-uncommitted and meiosis-committed stages. The mutant showed higher sensitivity to photoactivated bifunctional psoralen (8-MOP+UVA) during all stages of the meiotic cycle. Mutation induction by 3-CPs+UVA or 8-MOP+UVA in meiosis-committed cells revealed no significant differences between wild-type and thepso3-1 mutant. The status of thePSO3 gene has no influence on the kinetics of induction of gene conversion and crossing-over after 3-CPs+UVA treatment in meiosis-committed cells: gene conversion was blocked while recombination was induced. After treatment with 8-MOP+UVA gene conversion was also blocked in both strains while crossing-over could only be observed in meiosis-committed wild-type cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712961
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  • 12
    Electronic Resource
    Electronic Resource
    Basidiomycetousras cDNA functionally replaces its homolog genes in yeast (1994)
    Springer
    Current genetics 25 (1994), S. 30-33 
    Details
    ISSN: 1432-0983
    Keywords: Plasmid exchange ; ras/Ras gene ; Basidiomycete ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It was shown by a plasmid exchange procedure that the Ras-encoding cDNA of the basidiomyceteLentinus edodes (namedLeras cDNA) can functionally replace its homolog genes (ScRAS1 andScRAS2) in the yeastSaccharomyces cerevisiae to maintain the viability of an yeast strain containing genetic disruptions of bothRAS genes. The strain replaced by aLeras−cDNA-carrying plasmid, however, grew slower than the strains replaced by aScRAS1− or aScRAS2−carrying plasmid. The intracellular level of cAMP in the strain harboring theLeras−cDNA-carrying plasmid was clearly higher than that of a parental strain which maintains a plasmid carrying theS. cerevisiae cAMP-dependent protein kinase catalytic subunit C1 gene,TPK1, but was lower than that in a strain harboring anScRAS2−carrying plasmid. These results suggest that theLeras cDNA can complement theras1 − ras2− mutation of yeast by virture of the stimulation of adenylate cyclase activity, although the complementation is not as efficient as that obtained by expressing theScRAS2 gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712963
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  • 13
    Electronic Resource
    Electronic Resource
    Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination (1994)
    Springer
    Current genetics 25 (1994), S. 142-149 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Mitochondria ; DNA recombination ; 5′ exonuclease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mitochondrial DNA recombination was reduced in an yeast mutant lacking the NUC1 endo/exonuclease. Between linked markers in either the ω or cob region the frequency of recombination decreased nearly 50% compared to wild-type. Gene conversion frequencies in the var1 gene and in the ω region were also lower in the mutant strain. In particular, the gradient of gene conversion at ω was most affected by the absence of the NUC1 nuclease. In crosses between nuclease-deficient and wild-type strains, gene conversion frequencies at ω were reduced only when the ω+ allele was contributed to the zygote by the nuclease-deficient parent. We propose that the 5′ exonuclease activity of the NUC1 nuclease functions during recombination to enlarge heteroduplex tracts following a double-strand break in DNA. In crosses between nuclease-deficient and wild-type strains, the anisotropy in gene conversion frequencies at ω is hypothesized to be due to the slow mixing of parental motochondrial membranes as they fuse in the zygote.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309540
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  • 14
    Electronic Resource
    Electronic Resource
    New in-vivo cloning methods by homologous recombination in yeast (1994)
    Springer
    Current genetics 25 (1994), S. 180-183 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; In-vivo cloning ; Non-replicative vectors ; Homologous recombination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have devised a new strategy to clone DNA sequences from an yeast autonomously-propagating plasmid into a non-autonomous integrative vector by in-vivo recombination. The method consists of a first step in which the replicative plasmid carrying the DNA fragment of interest forms a co-integrate with the non-replicative plasmid by an induced in-vivo reciprocal exchange accompanied by gene conversion. The dimeric plasmid obtained is then purified and cut with an appropriate restriction enzyme and ligated independently to obtain the two intact monomeric plasmids, the original autonomous plasmid plus the new non-autonomous plasmid carrying the subcloned DNA fragment. The dimeric co-integrate can also serve as substrate for a second in-vivo reciprocal exchange that produces new autonomous plasmids carrying the desired DNA fragment. The technique considerably expands the applications of in-vivo cloning in yeast by complementing three important characteristics of previously published methods: (1) it can be used to clone into non-propagating vectors; (2) co-transformation experiments are not required; and (3) the intermediate co-integrate can be used to generate new types of autonomously-propagating plasmids directly. These characteristics are independent of whether the DNA insert is flanked by appropriate restriction sites or whether it does, or does not, express a detectable phenotype in yeast. The method is particularly useful for the cloning of large DNA fragments and can be used for plasmids from organisms other than yeasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309546
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  • 15
    Electronic Resource
    Electronic Resource
    Distinct upstream activation regions for glucose-repressed and derepressed expression of the yeast citrate synthase gene CIT1 (1994)
    Springer
    Current genetics 25 (1994), S. 185-195 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Citrate synthase ; Transcriptional regulation ; HAP2,3,4
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The yeast CIT1 (mitochondrial citrate synthase) gene is subject to glucose repression and is further repressed by glucose plus glutamate. Based on deletion analysis of a CIT1-lacZ gene fusion, DNA sequences between -548 and -273 are required for full expression of CIT1. The region of transcription initiation and the putative TATA element are located at -150 to -100 and -195 respectively. A restriction fragment containing DNA sequences between -457 and -211 conferred activation and glucose-glutamate regulation when placed in either orientation upstream of a USA-less heterologous yeast gene. Deletion of DNA sequences between -291 and -273 specifically eliminated derepression of CIT1, and destroyed one of two closely-spaced, potential binding sites for the HAP2,3,4 transcriptional activator protein. Tenbase-pair block substitutions in the region -367 to -348 reduced glucose-repressed expression. Thus, it appears that distinct DNA sequences upstream of CIT1 activate expression in glucose-repressed and derepressed cells. Possible mechanisms of regulation by glutamate plus glucose, are discussed.
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    URL: http://dx.doi.org/10.1007/BF00357161
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  • 16
    Electronic Resource
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    Cloning and analysis of a FLO5 flocculation gene from S. cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 196-201 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Flocculation ; Cloning ; Expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A yeast flocculation gene was isolated from a genomic library of an FLO5 strain of S. cerevisiae on the basis of its ability to trigger flocculation in a non-flocculent strain. Characterization of the cloned gene by restriction mapping, Southern analysis, and chromosome mapping have shown that it corresponds to a FLO5 gene previously located on chromosome I and that this gene is related to the already described. FLO1 gene. A study of gene expression in different yeast strains has indicated that, while this gene is dominant, its expression can be suppressed in some genetic backgrounds. A Northern-blot analysis has demonstrated that the same 5000-nt transcript was present in an FLO5 and an FLO1 strain. A gene disruption experiment has led to the conclusion that another flocculation gene is present and can be active in the FLO5 strain we used.
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    URL: http://dx.doi.org/10.1007/BF00357162
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  • 17
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    Expression of the Saccharomyces cerevisiae CYT2 gene, encoding cytochrome c1 heme lyase (1994)
    Springer
    Current genetics 25 (1994), S. 291-298 
    Details
    ISSN: 1432-0983
    Keywords: Cytochrome c 1 ; Cytochrome c 1 heme lyase ; GRF2p ; Glucose repression ; HAPp ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this paper we examine the expression of the Saccharomyces cerevisiae CYT2 gene, which encodes cytochrome c 1 heme lyase. This enzyme is required for covalent attachment of heme to apocytochrome c 1, a subunit of the mitochondrial respiratory chain. Transcription of the 1-kb CYT2 mRNA initiates at four prominent sites at a distance of 52–225 bp in front of the AUG start codon. The level of CYT2 mRNA is not influenced by the presence or absence of oxygen or of heme, but it is subject to carbonsource control. The concentration of the CYT2 mRNA is significantly reduced in glucose-grown cells as compared to cells grown under non-repressing conditions. Neither the HAPp activator proteins nor MIG1p, a repressor protein involved in glucose repression, seem to mediate this effect.
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    URL: http://dx.doi.org/10.1007/BF00351480
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  • 18
    Electronic Resource
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    PET112, a Saccharomyces cerevisiae nuclear gene required to maintain rho + mitochondrial DNA (1994)
    Springer
    Current genetics 25 (1994), S. 299-304 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; PET111 ; Translation ; COX2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear gene PET112 was originally identified by a mutation (pet112-1) that specifically blocked accumulation of cytochrome c oxidase subunit II. The mutation causes a post-transcriptional defect since the level of COX2 mRNA in the mutant is the same as in the wildtype. However, PET112 does not have a function similar to that of PET111, a COX2 mRNA-specific translational activator: while pet111 mutations are suppressed by chimeric COX2 mRNAs bearing 5′ leaders of other mitochondrial mRNAs, pet112-1 is not. The PET112 gene was isolated and shown to code a protein of 541 residues (62 kDa) with no significant homology to known amino-acid sequences. By hybridization to defined genomic clones the gene was mapped to chromosome II between cdc25 and ilsl. Disruption of the PET112 open reading frame destabilized the mitochondrial genome, causing cells to become rho-. This finding suggests that PET112 has an important general function in mitochondrial gene expression, probably in translation.
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    URL: http://dx.doi.org/10.1007/BF00351481
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  • 19
    Electronic Resource
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    Overexpression of the SNQ3/YAP1 gene confers hyper-resistance to nitrosoguanidine in Saccharomyces cerevisiae via a glutathione-independent mechanism (1994)
    Springer
    Current genetics 25 (1994), S. 469-471 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; GSH ; DNA alkylation ; MNNG
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The MNNG hyper-resistance of yeast transformants containing multiple copies of the SNQ3/YAP1 yeast gene is not caused by lowered MNNG activation due to depleted pools of glutathione. On the contrary, the SNQ3/YAP1-encoded protein stimulates production of GSH, apparently by promoter activation due to the AP-1 recognition element. Expression of at least one further gene, encoding a protein with a strong detoxifying activity, must also be stimulated to explain the MNNG hyper-resistance phenotype.
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    URL: http://dx.doi.org/10.1007/BF00351788
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  • 20
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    The Escherichia coli recA gene increases UV-induced mitotic gene conversion in Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 472-474 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; recA gene expression ; UV radiation ; Mitotic gene conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of the Escherichia coli RecA protein on mitotic recombination in the diploid D7 strain of Saccharomyces cerevisiae damaged by UV radiation was investigated. The D7 strain was transformed by two modified versions of the pNF2 plasmid: one, containing the ADH-1 promoter, and the other containing the recA gene tandemly arranged behind the ADH-1 promoter region. Immunological analysis proved the presence of the 38-kDa RecA protein in D7/pNF2ADHrecA transformants. We observed a positive effect of recA gene expression on mitotic gene conversion, mainly at higher doses of UV radiation. The results indicate that a RecA-like activity could participate in steps preceeding mitotic conversion events in yeast.
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    Comparative analysis of the region of the mitochondrial genome contaning the ATPase subunit 9 gene in the two related yeast species Saccharomyces douglasii and Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 504-507 
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    ISSN: 1432-0983
    Keywords: Yeast ; S. douglasii ; mtDNA evolution ; ATPase subunit 9
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have determined the nucleotide sequence of a region of the mitochondrial genome of the yeast Saccharomyces douglasii which contains the ATPase subunit 9 gene and part of the intergenic sequences that surround it. The gene is 228 nucleotides long and encodes a polypeptide of 76 aa. A comparison of the coding sequence with that of S. cerevisiae reveals the presence of three silent transitions. A high level of similarity is also found between regions involved in the initiation of transcription and mRNA processing. More interestingly, a region of similarity situated outside the known regulatory regions has been identified. As the intergenic regions are generally highly divergent, the remarkable conservation of these non-coding sequences suggests that their structure may be relevant to the expression of this region of the mitochondrial DNA.
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    Isolation and characterization of sulfite mutants of Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 488-496 
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    ISSN: 1432-0983
    Keywords: Sulfite ; Yeast ; Drug resistance ; Thioredoxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sulfite-resistant and sulfite-sensitive mutants of Saccharomyces cerevisiae were isolated and characterized. Genetic analysis indicated that one and four genes were responsible for the resistant and sensitive responses, respectively, and suggested that defects in methionine and cysteine metabolism were not involved. Some resistant alleles, all of which were dominant, conferred greater resistance than others. Mutations conferring sensitivity were recessive and one co-segregated with impaired respiration. Two of the sensitive mutants exhibited cross-sensitivity to other metabolic inhibitors: sulfometuron methyl, cycloheximide, oligomycin, and antimycin A. A 50% glutathione deficiency in one sensitive mutant was not sufficient in itself to account for its sensitivity. Screening of other relevant mutants revealed that relative to wild-type, met8 and a thioredoxin null mutant are sensitive, and met3 and met14 mutants are not. Reduced production of extracellular acetaldehyde, a compound that detoxifies sulfite, was observed in three of the four sensitive mutants. However, acetaldehyde was also underproduced in the resistant mutant. Because sulfite is a reducing agent, cells were tested for coincident sensitivity or resistance to ascorbate, selenite, dithiothreitol, nitrite, thiosulfate, reduced glutathione, and cysteine. No consistent pattern of responses to these agents emerged, suggesting that the response to sulfite is not a simple function of redox potential.
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    An analysis of the sequence of part of the right arm of chromosome II of S. cerevisiae reveals new genes encoding an amino-acid permease and a carboxypeptidase (1994)
    Springer
    Current genetics 26 (1994), S. 1-7 
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    ISSN: 1432-0983
    Keywords: Yeast ; Sequence ; Amino-Acid Permease ; Carboxypeptidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have analysed two new genes, YBR1007 and YBR1015, discovered during the systematic sequencing of chromosome II of S. cerevisiae. YBR1007 shows strong similarities to amino-acid permeases, in particular the high-affinity proline permeases of S. cerevisiae and A. nidulans. The number and position of the predicted membrane-spanning domains suggest a conserved structure for these proteins, with 12 trans-membrane domains. YBR1015 shows strong similarities to serine carboxypeptidases; all three residues of the “catalytic triad” typical of this family of enzymes are conserved in the YBR1015 protein. In a preliminary functional analysis we have created a null allele of the YBR1015 gene, and shown that it is not essential for cellular viability.
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    ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 26 (1994), S. 15-20 
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    ISSN: 1432-0983
    Keywords: Cell-division cycle ; Mitochondrial genome ; Nuclear mutation ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In former studies it was found that the ERV1 gene is essential for cell viability and for the biogenesis of functional mitochondria. A temperature-sensitive nuclear mutant exhibits a severe reduction in all the mitochondrial transcripts. Elimination of the gene leads to growth arrest after a few cell divisions. The putative gene product bears the characteristics of a regulatory factor since it has low expression rate and a high content of charged amino acids. In this study it is further verified that the ERV1 gene alone is responsible for the observed cellular and mitochondrial defects. The 5′ region of the gene is analysed by DNA deletions and complementation studies. Expression of the gene under the control of the GAL1-10 promoter in a disruption strain of ERV1 allows a more detailed specification of its influence on mitochondrial and cellular functions. Immediate and complete loss of mitochondrial genomes is observed after the promoter has been shut off, whereas the yeast cells are still able to grow for a limited time under these conditions. Analysis of the cells by in-vivo DNA flurorescence demonstrates a specific arrest in the cell-division cycle as the terminal phenotype. To further characterize the temperature-sensitive allele of ERV1 the mutated gene has been isolated and sequenced. A single point mutation which leads to the exchange of a single amino acid is found in the reading frame.
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    Analysis of meiotic recombination events near a recombination hotspot in the yeast Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 26 (1994), S. 21-30 
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    ISSN: 1432-0983
    Keywords: Recombination ; Yeast ; Cross-over ; Gene conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The region of yeast chromosome III between the HIS4 and LEU2 genes has an unusually high frequency of meiotic recombination. In order to determine the pattern of cross-over and gene conversion events, we constructed a strain with a number of heterozygous markers in this 25-kb interval. We found that very high levels of reombination are localized to regions of DNA near HIS4. In addition, analysis of the patterns of co-conversion of adjacent markers suggests that there is more than one initiation site contributing to recombination of HIS4.
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    The yeast nuclear gene MRP-L13 codes for a protein of the large subunit of the mitochondrial ribosome (1994)
    Springer
    Current genetics 26 (1994), S. 8-14 
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    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Nuclear gene ; Mitochondria ; Mitochondrial ribosomal protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear gene MRP-L13 of Saccharomyces cerevisiae, which codes for the mitochondrial ribosomal protein YmL13, has been cloned and characterized. It is a single-copy gene residing on chromosome XI. Its nucleotide sequence was found to be identical to that of the previously reported ORF YK105. A comparison of the predicted protein sequence of the MRP-L13 gene product and the actual N-terminal amino-acid sequence of the isolated YmL13 protein indicated that the mature protein is preceded by a mitochondrial signal peptide of 86 amino-acid residues, which is the longest among all known mitochondrial ribosomal proteins of S. cerevisiae. No sequence similarity was found to any other ribosomal protein in the current databases. The transcription of MRP-L13 was found to be repressed in the presence of glucose. Its protein product is not strictly essential for mitochondrial functions, but disruption of the gene by insertion of LEU2 noticeably affected cellular growth on non-fermentable carbon sources.
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    Formation of a minichromosome in Cryptococcus neoformans as a result of electroporative transformation (1994)
    Springer
    Current genetics 26 (1994), S. 54-61 
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    ISSN: 1432-0983
    Keywords: Transformation ; Minichromosome ; Yeast ; Cryptococcus neoformans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A minichromosome of approximately 270 kilobases was generated following complementation of a ura5 mutant strain of C. neoformans with the plasmid pURA5g2. This is the first report of the in-vivo generation of a minichromosome by the method of electroporative transformation. The minichromosome occurred at a relatively high (〉20%) frequency in transformants that were stable for uracil protoprophy. The minichromosome was maintained in linear form as a large extrachromosomal element of the normal karyotype. Gel-purified DNA from the minichromosome readily transformed the ura5 mutant of C. neoformans. Southern-blot analysis of the minichromosome revealed the presence of multiple copies of the URA5 gene and ribosomal DNA sequences in addition to containing telomere-like sequence repeats. The minichromosome was transmitted through mitosis and meiosis with extremely-high fidelity.
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    Mapping of additional markers in fission yeast, especially fus1 and three mfm genes (1994)
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    Current genetics 26 (1994), S. 187-189 
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    ISSN: 1432-0983
    Keywords: Mapping ; Yeast ; Schizosaccharomyces pombe
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The following genes of the fission yeast Schizosaccharomyces pombe have been mapped by tetrad analysis — chromosome arm I-L: mfm2, rad24, rad25; I-R: abc1, fus1, mfm1; II-L: mfm3; II-R: mam1, rad13. A hotspot of meiotic recombination although not quite so active as suggested by previous maps, may be located between rad25 and aro5 on I-L.
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    Evidence for a nucleotide-dependent topoisomerase activity from yeast mitochondria (1994)
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    Current genetics 27 (1994), S. 31-37 
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    ISSN: 1432-0983
    Keywords: Topoisomerase ; Mitochondria ; Nucleotides ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Yeast mitochondria were found to contain a novel topoisomerase-like activity which required nucleoside di- or tri-phosphates as a cofactor. ADP supported activity as effectively as ATP and the optimal concentration for each was approximately 20 μM. None of the other standard ribo- or deoxyrib-onucleotides could fully substitute for either ADP or ATP. The non-hydrolyzable ATP analogs, adenosine-5′-0-(3-thiotriphosphate) (ATP-γ-S), adenylyl (β, γ-methylene) (AMP-PCP), and andenyl-imidodiphosphate (AMP-PNP) also supported activity suggesting that the nucleotide cofactor regulated topoisomerase activity rather than serving as an energy donor in the reaction. The mitochondrial topoisomerase activity relaxed both positively and negatively supercoiled DNA. It was not inhibited by concentrations of ethidium bromide up to 2 μg/ml nor by either nalidixic or oxolinic acids; novobiocin, coumermycin, and berenil inhibited the activity. Genetic and biochemical analysis of the mitochondrial topoisomerase activity indicated that it was not encoded by the nuclear TOP1, TOP2, and TOP3 genes.
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    Antisense RNA regulation of the ILV2 gene in yeast: a correction (1994)
    Springer
    Current genetics 25 (1994), S. 289-289 
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    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Inducible antisense gene ; Acetolactate synthase ; Bradytrophic phenocopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A previous report of the use of antisense RNA to regulate gene expression in yeast is incorrect.
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    Approaching the function of new genes by detection of their potential upstream activation sequences in Saccharomyces cerevisiae: application to chromosome III (1994)
    Springer
    Current genetics 25 (1994), S. 396-406 
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    ISSN: 1432-0983
    Keywords: Yeast ; Regulation ; UAS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The systematic sequencing of the yeast genome reveals the presence of many potential genes of unknown function. One way to approach their function is to define which regulatory system controls their transcription. This can also be accomplished by the detection of an upstream activation sequence (UAS). Such a detection can be done by computer, provided that the definition of a UAS includes sufficient and precise rules. We have established such rules for the UASs of the GAL4, RAP1 (RPG box), GCN4, and the HAP2/HAP3/HAP4 regulatory proteins, as well as for a motif (PAC) frequently found upstream of the genes of the RNA polymerase A and C subunits. These rules were applied to the chromosome III DNA sequence, and gave precise predictions.
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    Isolation and characterization of three mutants with increased sensitivity to photoactivated 3-carbethoxypsoralen in Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 407-411 
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    ISSN: 1432-0983
    Keywords: Psoralen sensitivity ; Saccharomyces cerevisiae ; DNA repair ; Oxidative stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The complementation and genetical analysis of yeast mutants sensitive to photoactivated 3-carbethoxy-psoralen define three novel recessive mutant alleles pso-5-1, pso6-1, and pso7-1. Their cross-sensitivity to UV254nm, radiomimetic mutagens, and to chemicals enhancing oxidative stress suggest that these mutants are either impaired in metabolic steps protecting from oxidative stress or in mechanisms of the repair of oxygen-dependent DNA lesions. None of the three novel mutant alleles block the induction of reverse mutation by photoactivated mono- and bi-functional psoralens, nitrogen mustards, or UV254nm.
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    Suppression of a mitochondrial point mutation in a tRNA gene can cast light on the mechanisms of 3′ end-processing (1994)
    Springer
    Current genetics 25 (1994), S. 451-455 
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    ISSN: 1432-0983
    Keywords: tRNA processing ; Saccharomyces cerevisiae ; Mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We used a genetic approach to study the nuclear factors involved in the biogenesis of mitochondrial tRNAs. A point mutation in the mitochondrial tRNAAsp gene of Saccharomyces cerevisiae had previously been shown to result in a temperature-sensitive respiratory-deficient phenotype as a result of the absence of 3′ end-processing of the tRNAAsp. Analysis of mitochondrial revertants has shown that all revertants sequenced have a G-A compensatory change at position 53, which restores the hydrogen-bond with the mutated nucleotide. We then searched for nuclear suppressors to identify the nuclear gene(s) involved in mitochondrial tRNA 3′ end-processing. One such suppressor mutation was further characterized: it restores tRNAAsp maturation and growth at 36°C on glycerol medium in heterozygous diploids, but leads to a defective growth phenotype in haploids.
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    Stabilization of methionine-rich protein in Saccharomyces cerevisiae: targeting of BZN protein into the peroxisome (1994)
    Springer
    Current genetics 26 (1994), S. 390-397 
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    ISSN: 1432-0983
    Keywords: Overexpression ; Peroxisomes ; Saccharomyces cerevisiae ; Stabilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have constructed a gene coding for the 12-kDa intermediate form of the 2s methionine-rich protein from Bertholletia excelsa seeds. This protein, expressed intracellularly in yeast, is characterised by a 20-min balf-life. By adding 11 amino acids corresponding to the peroxisome-targeting sequence (PTSc) of luciferase, we have significantly increased its half-life. This stabilization allowed accumulation of the BZN protein into the peroxisome as judged by cell fractionation. Accumulation of the 12-kDa protein results in a significant increase of the total methionine content in yeast cells (30%) indicating that such a microorganism could represent a practicable protected shuttl for an animal-feed additive.
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    A 61-kb ring chromosome shows an ARS-dependent increase in its mitotic stability in the mcm2 mutant of yeast (1994)
    Springer
    Current genetics 26 (1994), S. 403-409 
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    ISSN: 1432-0983
    Keywords: Yeast ; DNA replication ; mcm ; Chromosome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have studied the effects of ARS addition and deletion on the maintenance of a 61-kb ring derivative of chromosome III in a minichromosome maintenance mutant of yeast carrying the mcm2-1 mutation. When this ring chromosome, CIIIR, had either of its two strong origins deleted, the resultant chromosome showed a much greater instability in the mutant as compared to that of the wild-type strain. Integration of more ARSs improved the maintenance of CIIIR in the mutant but not in the wild-type strain. Increase in the size of CIIIR, without any ARS addition, did not improve the stability in either strain. A spontaneous revertant for improved growth at 35°C also co-reverted for minichromosome and CIIIR maintenance. The results suggest that ARS malfunctioning leads to minichromosome and chromosome loss from mutant cells, affecting their growth at higher temperatures.
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    Sequence analysis of three deficient mutants of cytochrome oxidase subunit I of Saccharomyces cerevisiae and their revertants (1994)
    Springer
    Current genetics 26 (1994), S. 546-552 
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    ISSN: 1432-0983
    Keywords: Cytochrome oxidase ; Revertant ; Mitochondria ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three respiratory-deficient mutants of cytochrome oxidase subunit I in the yeast mitochondrion have been sequenced. They are located in, or near, transmembrane segment VI, the catalytic core of the enzyme. Respiratory-competent revertants have been selected and studied. The mutant V244M was found to revert at the same site in valine (wild-type), isoleucine or threonine. The revertants of the mutant G251R were of three types: glycine (wild-type), serine and threonine at position 251. A search for second-site mutations was carried out but none were found. Among 60 revertants tested, the mutant K265M was found to revert only to the wild-type allele.
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    Molecular characterisation of GTP1, a Saccharomyces cerevisiae gene encoding a small GTP-binding protein (1994)
    Springer
    Current genetics 26 (1994), S. 564-566 
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    ISSN: 1432-0983
    Keywords: Small GTP-binding proteins ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract DNA sequence analysis upstream of the yeast DNA repair gene SNM1 revealed gene GTP1 with an ORF of 573 bp on chromosome XIII. The putative amino-acid sequence of the encoded protein shows homology to proteins of the ARF-class of small GTP-binding proteins. Homology within GTP-binding motifs is highly conserved. Gene disruption showed that GTP1 is not an essential gene and that it has no influence on the expression of the DNA repair gene SNM1 with which it shares a 191-bp promoter region.
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    Identification of extragenic suppressors of the cif1 mutation in Saccharomyces cerevisiae (1994)
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    Current genetics 25 (1994), S. 89-94 
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    ISSN: 1432-0983
    Keywords: cif1 ; Suppressor ; Trehalose ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cif1 mutation of Saccharomyces cerevisiae causes inability to grow on glucose and related fermentable carbon sources. We have isolated two different suppressor mutations that allow growth on glucose of yeasts carrying the cif1 mutation. One of them, sci1-1, is recessive and caused inability to grow on non-fermentable carbon sources and to de-repress fructose-1,6-bisphosphatase. The other suppressor mutation, SCI2-1, is dominant and diminished the capacity to phosphorylate glucose or fructose. The SCI2-1 mutation decreased sporulation efficiency by 70% in heterozygosis and by more than 90% in homozygosis. In a CIF1 background, cells carrying the mutation SCI2-1 accumulated trehalose during the logarithmic phase of growth and hyperaccumulated it during the stationary phase. Genetic tests showed that SCI2 was either allelic, or else closely linked, to HXK2. The concentrations of the glycolytic metabolites measured during growth on glucose in cells carrying the cif1 mutation and any of the suppressor mutations were similar to those of a wild-type. Both types of suppressor mutations restored the transient cAMP response to glucose to cif1 mutants.
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    Identification of the yeast ACC1 gene product (acetyl-CoA carboxylase) as the target of the polyketide fungicide soraphen A (1994)
    Springer
    Current genetics 25 (1994), S. 95-100 
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    ISSN: 1432-0983
    Keywords: Acetyl-CoA carboxylase ; Polyketide antibiotic ; Soraphen A ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Soraphen A, a polyketide isolated from the myxobacterium Sorangium cellulosum, is a potent inhibitor of fungal growth. We have used a genetic approach to localize the target of this drug, employing Saccharomyces cerevisiae as a model organism. We have isolated soraphen A-resistant mutants and found that all of them map at the same genetic locus and exhibit a broad range of semidominant phenotypes. Data from genetic crosses of soraphen A-resistant clones with an acc1 mutant revealed that ACC1, coding for acetyl-CoA carboxylase (E.C. 6.4.1.2), is tightly linked to soraphen A resistance. Partially-purified enzyme extracts containing acetyl-CoA carboxylase were prepared and assayed for their soraphen A sensitivity. Our experiments showed that the catalytic activity of the wild-type enzyme is inhibited in vitro by soraphen A while the mutant enzyme remains catalytically active. Taken together these data strongly suggest that the ACC1 gene product is the primary target for soraphen A in vivo.
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    Yeast ts secretory mutation rgs1 is suppressed by the SEC4 gene of Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 178-179 
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    ISSN: 1432-0983
    Keywords: Yeast ; Secretion ; Vesicle fusion ; Rabproteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Yeast rgs1 cells accumulate secretory vesicles in the cytoplasm and stop the secretion of proteins at the restrictive temperature. The ts mutation rgs1 may be suppressed by several different genes; the S. cerevisiae SEC4 gene, encoding the small G-protein involved in the late secretory stage, is one of them. Synthetic lethality of the double rgs1 sec4 mutant is demonstrated.
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    Kinetic studies of killer toxin K1 binding to yeast cells indicate two receptor populations (1994)
    Springer
    Archives of microbiology 162 (1994), S. 211-214 
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    ISSN: 1432-072X
    Keywords: Killer toxin ; Saccharomyces cerevisiae ; Toxin binding ; Cell wall receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A recently described new method for determination of killer toxin activity was used for kinetic measurenments of K1 toxin binding. The cells of the killer sensitive strain Saccharomyces cerevisiae S6 were shown to carry two classes of toxin binding sites differing widely in their half-saturation constants and maximum binding rates. The low-affinity and high-velocity binding component (K T1=2.6x109 L.U./ml, V max1=0.19 s-1) probably reflects diffusion-limited binding to cell wall receptors; the high-affinity and low-velocity component (K T2=3.2x107 L.U./ml, V max2=0.03 s-1) presumably indicates the binding of the toxin to plasma membrane receptors. Adsorption of most of the killer toxin K1 to the surface of sensitive cells occured within 1 min and was virtually complete within 5 min. The amount of toxin that saturated practically all cell receptors was about 600 lethal units (L.U.) per cell of S. cerevisiae S6.
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    Effect of the new fluorescent brightener Rylux BSU on morphology and biosynthesis of cell walls in Saccharomyces cerevisiae (1994)
    Springer
    Archives of microbiology 161 (1994), S. 340-344 
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    ISSN: 1432-072X
    Keywords: Rylux BSU ; Fluorescent brightener ; Cell walls ; Chitin synthase ; Glucan synthase ; Yeast ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rylux BSU, a new fluorescent brightener from the family of 4,4′-diaminostilbene-2,2′disulfonic acid derivatives, inhibited growth and cytokinesis of the yeast Saccharomyces cerevisiae. In the presence of 0.1–1 mg/ml Rylux BSU the cells grew in clumps, had irregular shape and were larger than controls. They formed apparently normal primary septa but their secondary septa and lateral cell walls, especially those in older cells, were abnormally thick with large deposits of amorphous wall material in the periplasmic spaces all over the cell surface. Chitin content in the cell walls of cells grown in the presence of Rylux BSU was increased 2 to 5 times in comparison to that of the controls and glucan content was reduced by up to 30%. In the in vitro assays with particulate membrane fractions, Rylux BSU acted as a non-competitive inhibitor of β-1,3-glucan synthase with inhibitory constant K i=1.75 mg/ml whereas the chitin synthase was inhibited to a much lesser extent. From the difference of the effects of Rylux BSU on the synthesis of chitin in vivo and in vitro it is concluded that the brightener interacts with chitin synthase only indirectly, possibly by influencing the properties of integral plasma membrane.
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    Kinetic studies of killer toxin K1 binding to yeast cells indicate two receptor populations (1994)
    Springer
    Archives of microbiology 162 (1994), S. 211-214 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Killer toxin ; Saccharomyces cerevisiae ; Toxin binding ; Cell wall receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      A recently described new method for determination of killer toxin activity was used for kinetic measurements of K1 toxin binding. The cells of the killer sensitive strain Saccharomyces cerevisiae S6 were shown to carry two classes of toxin binding sites differing widely in their half-saturation constants and maximum binding rates. The low-affinity and high-velocity binding component (K T1 = 2.6 × 109 L.U./ml, V max1 = 0.19 s– 1) probably reflects diffusion-limited binding to cell wall receptors; the high-affinity and low-velocity component (K T2 = 3.2 × 107 L.U./ml, V max2 = 0.03 s– 1) presumably indicates the binding of the toxin to plasma membrane receptors. Adsorption of most of the killer toxin K1 to the surface of sensitive cells occured within 1 min and was virtually complete within 5 min. The amount of toxin that saturated practically all cell receptors was about 600 lethal units (L.U.) per cell of S. cerevisiae S6.
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    Phytate dephosphorylation by free and immobilized cells ofSaccharomyces cerevisiae (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 30-34 
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    ISSN: 1476-5535
    Keywords: Phytate ; Saccharomyces cerevisiae ; Polyacrylamide gel ; Inositol phosphates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Saccharomyces cerevisiae in the form of baker's yeast, cells cultivated on a yeast extract-peptone-glucose medium, as well as cells immobilized in 18% (w/v) polyacrylamide gel showed the ability to hydrolyze 1.727 mM sodium phytate solution at 45°C, pH 4.6, in a stirred tank reactor. Seventy percent yield of dephosphorylation was observed after 2 h using a baker's yeast concentration of 5.8 g dry matter per 100 ml. Hydrolytic activity at 1.8–2.0 μM Pi min−1 was observed between 1st and 3rd h of the reaction in cells cultured 24 or 48 h. No inhibition by the substrate was found at sodium phytate concentrations of 0.587–1.727 mM. After 1.5 h of hydrolysis a single, well distinguished peak ofmyo-inositol-triphosphate was the main product found. By means of immobilization the stability of the biocatalyst was enhanced 3.3-fold and reached its half-life at 64 ninety-minute runs.
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    Evolution of C6, C8 and C10 acids and their ethyl esters in cells and musts during fermentation with threeSaccharomyces cerevisiae races (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 269-272 
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    ISSN: 1476-5535
    Keywords: Wine ; Yeasts ; Fatty acids ; Ethyl esters ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The evolution of the cell and must contents of three short-chain fatty acids (C6, C8 and C10) and their ethyl esters during fermentations withSaccharomyces cerevisiae racescerevisiae, bayanus andcapensis were studied. The former is a fermentative yeast and the last two are ‘flor’ film yeasts. The acid concentrations in the musts increased throughout the alcoholic fermentations, and maximum cell concentrations of the fatty acids were reached after 48 h of fermentation. Maximum ester concentrations in the cells were attained after 48–72 h of fermentation. In the musts, ethyl octanoate and ethyl decanoate reached a peak also at this point, and ethyl hexanoate after 10 days. After 134 days,S. cerevisiae racecapensis formed a thick ‘flor’ film whileS. cerevisiae racebayanus developed a thin film andS. cerevisiae racecerevisiae formed no film. At this point, acid contents remained constant in the wines produced byS. cerevisiae racescerevisiae andbayanus, and decreased in those obtained with racecapensis. The ethyl ester contents tended to decrease with the exception of ethyl decanoate in the fermentations carried out byS. cerevisiae racescerevisiae andbayanus.
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    Glycerol production from sugars with phosphoglycerate mutasedeficientSaccharomyces cerevisiae partially resistant to glucose repression (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 17-23 
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    ISSN: 1476-5535
    Keywords: Yeast ; Glycerol production ; Low alcohol content wine ; Enology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Mutants partially resistant to the repressive effect of glucose have been isolated from aSaccharomyces cerevisiae strain totally deficient in phosphoglycerate mutase activity (EC 5.4.2.1) by a selection procedure involving the catabolite-repressive effect of 5-thio-d-glucose (5TG). These mutants are able to resist glucose concentrations up to 15 g L−1 and exhibit several non-repressed metabolic pathways such as gluconeogenesis, glyoxylic shunt or mitochondrial respiratory chain. Moreover, when these mutants are grown in aerobiosis on ethanol and glucose as sole substrates, glucose is mainly converted into glycerol in order to maintain a normal redox balance. Optimal glucose and oxygen concentrations have been defined for resting cells in order to obtain a glycerol yield from glucose close to 100%. The physiological characteristics of one of these mutants led us to consider an application of this yeast strain in reducing the ethanol content of wines previously lowered in ethanol content by physical processes.
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    Effect of the support matrix on biotransformation of benzaldehyde to benzyl alcohol by yeast cells in aqueous and aqueous-organic two phase systems (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 172-176 
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    ISSN: 1476-5535
    Keywords: Immobilization ; Hydrophobic ; Hydrophilic ; Polymers ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Biotransformation of benzaldehyde to benzyl alcohol bySaccharomyces cerevisiae immobilized in different support matrices was investigated. Polymers with intrinsic hydrophobic and/or hydrophilic nature as well as mixed hydrophobic and hydrophilic supports were examined both in aqueous and bisphasic aqueous-organic systems. The hydrophobic support material ENTP-2000 or mixed silicone:alginate (50-25∶50-75) proved to be most suitable not only for nonconventional media but also for conventional aqueous media for production of benzyl alcohol. With ENTP-2000, catalytic activity and maximum yield were 159 μmol h−1 g−1 dry weight catalyst and 0.89 mM, respectively, in hexane containing 2% moisture. Corresponding values in aqueous media were 246 μmol h−1 g−1 dry weight catalyst and 1.53 mM. With 50∶50 silicone:alginate, catalytic activity and maximum yield were 177 μmol h−1 g−1 dry weight catalyst and 1.18 mM, respectively, in hexane containing 2% moisture. Corresponding values in aqueous media were 192 μmol h−1 g−1 dry weight catalyst and 0.8 mM.
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    Isolation and characterization of a multienzyme complex containing DNA replicative enzymes from mitochondria ofS. cerevisiae (1994)
    Springer
    Molecular biology reports 20 (1994), S. 135-141 
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    ISSN: 1573-4978
    Keywords: mitochondria ; multienzyme complex ; replication ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 40 S multienzyme complex containing mtDNA polymerase was isolated from mitochondria ofS. cerevisiae by density gradient centrifugation and by gel filtration chromatography. Besides DNA polymerase, RNA polymerase, primase, 3′→5′ exonuclease and an ATPase activities were found to be associated with it. The presence of some of these enzymes were confirmed by Western blot. This high molecular weight multienzyme complex containing DNA has most of the attributes of a putative replisome.
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    Cloning of an Arabidopsis thaliana cDNA coding for farnesyl diphosphate synthase by functional complementation in yeast (1994)
    Springer
    Plant molecular biology 26 (1994), S. 1867-1873 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; cDNA ; complementation ; erg20-2 yeast mutant ; farnesyl diphosphate synthase ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA encoding farnesyl diphosphate synthase, an enzyme that synthesizes C15 isoprenoid diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate, was cloned from an Arabidopsis thaliana cDNA library by complementation of a mutant of Saccharomyces cerevisiae deficient in this enzyme. The A. thaliana cDNA was also able to complement the lethal phenotype of the erg20 deletion yeast mutant. As deduced from the full-length 1.22 kb cDNA nucleotide sequence, the polypeptide contains 343 amino acids and has a relative molecular mass of 39689. The predicted amino acid sequence presents about 50% identity with the yeast, rat and human FPP synthases. Southern blot analyses indicate that A. thaliana probably contains a single gene for farnesyl diphosphate synthase.
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    Dependence of the kinetics of secondary active transports in yeast on H+-ATPase acidification (1994)
    Springer
    The journal of membrane biology 138 (1994), S. 29-35 
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    ISSN: 1432-1424
    Keywords: H+ symports ; Plasma membrane ATPase ; Local vs. delocalized protons ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Acidification of the external medium of the yeast Saccharomyces cerevisiae, mainly caused by proton extrusion by plasma membrane H+-ATPase, was inhibited to different degrees by D2O, diethylstilbestrol, suloctidil, vanadate, erythrosin B, cupric sulfate and dicyclohexylcarbodiimide. The same pattern of inhibition was found with the uptake of amino acids, adenine, uracil, and phosphate and sulfate anions. An increase of the acidification rate by dioctanoylglycerol also increased the rates of uptake of adenine and of glutamic acid. In contrast, a decrease of the membrane potential at pH 4.5 from a mean of -40 to -20 mV caused by 20 mm KC1 had no effect on the transport rates. The ATPase-deficient mutant S. cerevisiae pmal-105 showed a markedly lower uptake of all the above solutes as compared with the wild type, while its membrane potential and ΔpH were unchanged. Other types of acidification (spontaneous upon suspension; K+ stimulated) did not affect the secondary uptake systems. A partially competitive inhibition between some individual transport systems was observed, most pronouncedly with adenine as the most avidly transported solute. These observations, together with the earlier results that inhibition of H+-ATPase activity affects more the acidic than the basic amino acids and that it is more pronounced at higher pH values and at greater solute concentrations, support the view that it is the protons in or at the membrane, as they are extruded by the ATPase, that govern the rates of uptake by secondary active transport systems in yeast.
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    Cytokeratin 18 is an M-cell marker in porcine Peyer's patches (1994)
    Springer
    Cell & tissue research 276 (1994), S. 213-221 
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    ISSN: 1432-0878
    Keywords: Gut-associated lymphoid tissue (GALT) ; M(membranous)-cells ; Immunohistochemistry ; Cytokeratins ; Yeast ; Pig (Minipig, Göttingen)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The intermediate filaments of the dome epithelium of porcine Peyer's patches were studied by immunohistochemistry. The labelling patterns of monospecific antibodies directed against cytokeratins 8, 18 and 19 differed considerably. About 40% of the dome epithelial cells were intensely labelled by three different anti-cytokeratin 18 antibodies, indicating that large amounts of cytokeratin 18 are present in these cells. In order to verify that these cytokeratin-18-immunoreactive cells were M-cells, uptake studies using fluorescein-labelled yeast particles were performed. Numerous yeast particles were found exclusively in dome epithelial cells that were highly positive for cytokeratin 18, thus representing M-cells. In contrast, the content of cytokeratin 19 in M-cells was lower than that in neighbouring enterocytes. The labelling intensity of cytokeratin 8 did not differ between M-cells and enterocytes. In addition, the absence of vimentin and desmin from the dome epithelium of porcine Peyer's patches was demonstrated. The results show (1) that porcine M-cells differ from enterocytes in the composition of their cytoskeleton, (2) that cytokeratin 18 is a useful marker for detecting porcine M-cells and (3) that this marker directly correlas with M-cell function.
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    Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered fatty acid synthase gene (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 90-96 
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    ISSN: 1617-4623
    Keywords: Cerulenin ; Saccharomyces cerevisiae ; Fatty acid synthase ; β-Ketoacyl synthase ; Drug resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cerulenin, an antifungal antibiotic produced by Cephalosporium caerulens, is a potent inhibitor of fatty acid synthase in various organisms, including Saccharomyces cerevisiae. The antibiotic inhibits the enzyme by binding covalently to the active center cysteine of the condensing enzyme domain. We isolated 12 cerulenin-resistant mutants of S. cerevisiae following treatment with ethyl methanesulfonate. The mechanism of cerulenin resistance in one of the mutants, KNCR-1, was studied. Growth of the mutant was over 20 times more resistant to cerulenin than that of the wild-type strain. Tetrad analysis suggested that all mutants mapped at the same locus, FAS2, the gene encoding the α subunit of the fatty acid synthase. The isolated fatty acid synthase, purified from the mutant KNCR-1, was highly resistant to cerulenin. The cerulenin concentration causing 50% inhibition (IC50) of the enzyme activity was measured to be 400 μM, whereas the IC50 value was 15 μM for the enzyme isolated from the wild-type strain, indicating a 30-fold increase in resistance to cerulenin. The FAS2 gene was cloned from the mutant. Sequence replacement experiments suggested that an 0.8 kb EcoRV-HindIII fragment closely correlated with cerulenin resistance. Sequence analysis of this region revealed that the GGT codon encoding Gly-1257 of the FAS2 gene was altered to AGT in the mutant, resulting in the codon for Ser. Furthermore, a recombinant FAS2 gene, in which the 0.8 Kb EcoRV-HindIII fragment of the wild-type FAS2 gene was replaced with the same region from the mutant, when introduced into FAS2-defective S. cerevisiae complemented the FAS2 pheno-type and showed cerulenin resistance. These data indicate that one amino acid substitution (Gly → Ser) in the α subunit of fatty acid synthase is responsible for the cerulenin resistance of the mutant KNCR-1.
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    Increase in incidence of chromosome instability and non-conservative recombination between repeats in Saccharomyces cerevisiae hpr1Δ strains (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 224-236 
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    ISSN: 1617-4623
    Keywords: DNA deletions ; Reciprocal exchange ; Non-conservative recombination ; Yeast ; hpr1 Δ mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Null hprl Δ strains show a large increase (up to 2000-fold) over wild type in the frequency of occurrence of deletions between direct repeats on three different chromosomes. However, we show that hprl Δ mutations have little or no effect on reciprocal exchange, gene conversion or unequal sister chromatid exchange, as determined using intrachromosomal, interchromosomal and plasmid-chromosome assay systems. A novel intrachromosomal recombination system has allowed us to determine that over 95% of deletions in hpr1 Δ strains do not occur by reciprocal exchange. On the other hand, hpr1 Δ strains show chromosome loss frequencies of up to 100 times the wild-type level. Our results suggest that yeast cells have a very efficient non-conservative recombination mechanism, dependent on RADI and RAD52, that causes deletions between direct DNA repeats, and this mechanism is strongly stimulated in hpr1 Δ strains. The results indicate that the Hpr1 protein is required for stability of DNA repeats and chromosomes. We propose that in the absence of the Hprl protein the cell destabilizes the genome by allowing the initiation of events that lead to deletions of sequences between repeats, and to chromosome instability. We discuss the roles that proteins such as Hprl have in maintaining direct repeats and in preventing non-conservative recombination and consider the importance of these functions for chromosome stability.
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    Positive and negative transcriptional regulation by the yeast GAL11 protein depends on the structure of the promoter and a combination of cis elements (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 301-312 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcriptional regulation ; Chromatin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract GAL11 was first identified as a gene required for full expression of some galactose-inducible genes that are activated by GAL4, and it was subsequently shown to be necessary for full expression of another set of genes activated by RAP1/GRFl/TUF. Genetic analysis suggests that GAL11 functions as a coactivator, mediating the interaction of sequence-specific activators with basal transcription factors. To test this hypothesis, we first tried to identify functional domains by deletion analysis and found that the 866–910 region is indispensable for function. Using reporters bearing various upstream activating sequences (UAS) and different core promoter structures, we show that the involvement of GAL11 in transcriptional activation varies with the target promoter and the particular combination of cis elements. Gel electrophoresis in the presence of chloroquine shows that GAL11 affects the chromatin structure of a circular plasmid. Based on these findings, the role of GAL 11 in regulation of transcription, including an alteration in chromatin structure, is discussed.
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    Mating type regulates the radiation-associated stimulation of reciprocal translocation events in Saccharomyces cerevisiae (1994)
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    Molecular genetics and genomics 243 (1994), S. 63-70 
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    ISSN: 1617-4623
    Keywords: Radiation ; Reciprocal translocations ; MAT ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Both ultraviolet (UV) and ionizing radiation were observed to stimulate mitotic, ectopic recombination between his3 recombinational substrates, generating reciprocal translocations in Saccharomyces cervisiae (yeast). The stimulation was greatest in diploid strains competent for sporulation and depends upon both the ploidy of the strain and heterozygosity at the MAT locus. The difference in levels of stimulation between MATa/MATα diploid and MATα haploid strains increases when cells are exposed to higher levels of UV radiation (sevenfold at 150 J/m2), whereas when cells are exposed to higher levels of ionizing radiation (23.4 krad), only a twofold difference is observed. When the MATα gene was introduced by DNA transformation into a MATa/matα::LEU2 + diploid, the levels of radiation-induced ectopic recombination approach those obtained in a strain that is heterozygous at MAT. Conversely, when the MATA gene was introduced by DNA transformation into a MATα haploid, no enhanced stimulation of ectopic recombination was observed when cells were irradiated with ionizing radiation but a threefold enhancement was observed when cells were irradiated with UV The increase in radiation-stimulated ectopic recombination resulting from heterozygosity at MAT correlated with greater spontaneous ectopic recombination and higher levels of viability after irradiation. We suggest that MAT functions that have been previously shown to control the level of mitotic, allelic recombination (homolog recombination) also control the level of mitotic, radiation-stimulated ectopic recombination between short dispersed repetitive sequences on non-homologous chromosomes.
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    Increases in cell size at START caused by hyperactivation of the cAMP pathway in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 158-165 
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    ISSN: 1617-4623
    Keywords: Yeast ; Cell cycle ; Size control ; cAMP G1 cyclin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the budding yeast Saccharomyces cerevisiae, passage through START, which commits cells to a new round of cell division, requires growth to a critical size. To examine the effect of hyperactivation of the cAMP pathway on cell size at START, a strain was constructed that is able to respond to exogenously added cAMP. In the presence of cAMP, this strain showed increased cell volume at bud emergence, suggesting that the critical cell size necessary for START is increased. In addition, a mutation that results in unregulated cAMP-dependent protein kinase (bcy1) caused increased cell size at START. These results indicate that hyperactivation of the cAMP pathway causes increases in cell size through cAMP-dependent protein kinase. Cells carrying a hyperactive allele of CLN3 (CLN3-2) also showed increased size at START in the presence of cAMP. These cells retained resistance to α factor, however, suggesting that increases in cell size by cAMP are not due to a reduction of Cln3 activity. The observed increases in cell size due to hyperactivation of the cAMP pathway suggest that cell size modulation by nutrient conditions may be associated with a change of the activity of the cAMP pathway.
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    Prevalence and distribution of introns in non-ribosomal protein genes of yeast (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 532-539 
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    ISSN: 1617-4623
    Keywords: Yeast ; prp2 ; Intron ; Genome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Relatively few genes in the yeast Saccharornyces cerevisiae are known to contain intervening sequences. As a group, yeast ribosomal protein genes exhibit a higher prevalence of introns when compared to non-ribosomal protein genes. In an effort to quantify this bias we have estimated the prevalence of intron sequences among non-ribosomal protein genes by assessing the number of prp2-sensitive mRNAs in an in vitro translation assay. These results, combined with an updated survey of the GenBank DNA database, support an estimate of 2.5% for intron-containing non-ribosomal protein genes. Furthermore, our observations reveal an intriguing distinction between the distributions of ribosomal protein and non-ribosomal protein intron lengths, suggestive of distinct, gene class-specific evolutionary pressures.
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    SCM2, a tryptophan permease in Saccharomyces cerevisiae, is important for cell growth (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 260-268 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Amino acid permeases ; Transport ; Tryptophan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract SCM2, a novel gene encoding a yeast tryptophan permease, was cloned as a high-copy-number suppressor of cse2-1. The cse2-1 mutation causes cold sensitivity, temperature sensitivity and chromosome missegregation. However, only the cold-sensitive phenotype of cse2-1 cells is suppressed by SCM2 at high copy. SCM2 is located on the left arm of yeast chromosome XV, adjacent to SUP3 and encodes a 65 kDa protein that is highly homologous to known amino acid permeases. Four out of five disrupted scm2 alleles (scm2Δ1-Δ4) cause slow growth, whereas one disrupted allele (scm2Δ5) is lethal. Cells with both the scm2Δ1 and trp1-Δ101 mutations exhibit a synthetic cold-sensitive phenotype and grow much more slowly at the permissive temperature than cells with a single scm2Δ1 or trp1-Δ101 mutation. A region of the predicted SCM2 protein is identical to the partial sequence recently reported for the yeast tryptophan permease TAP2, indicating that SCM2 and TAP2 probably encode the same protein.
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    The Saccharomyces cerevisiae SGE1 gene product: a novel drug-resistance protein within the major facilitator superfamily (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 287-294 
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    ISSN: 1617-4623
    Keywords: Drug sensitivity ; Saccharomyces cerevisiae ; Major facilitator superfamily ; Drug expulsion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several pleiotropic drug sensitivities have been described in yeast. Some involve the loss of putative drug efflux pumps analogous to mammalian P-glycoproteins, others are caused by defects in sterol synthesis resulting in higher plasma membrane permeability. We have constructed a Saccharomyces cerevisiae strain that exhibits a strong crystal violet-sensitive phenotype. By selecting cells of the supersensitive strain for normal sensitivity after transformation with a wild-type yeast genomic library, a complementing 10-kb DNA fragment was isolated, a 3.4-kb subfragment of which was sufficient for complementation. DNA sequence analysis revealed that the complementing fragment comprised the recently sequenced SGE1 gene, a partial multicopy suppressor of gal11 mutations. The supersensitive strain was found to be a sge1 null mutant. Overexpression of SGE1 on a high-copy-number plasmid increased the resistance of the supersensitive strain. Disruption of SGE1 in a wild-type strain increased the sensitivity of the strain. These features of the SGE1 phenotype, as well as sequence homologies of SGE1 at the amino acid level, confirm that the Sge1 protein is a member of the drug-resistance protein family within the major facilitator superfamily (MFS).
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    Interactions between gene products involved in divalent cation transport in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 303-311 
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    ISSN: 1617-4623
    Keywords: Metal homeostasis ; Metal resistance ; Transport ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The COT1 and ZRC1 genes of Saccharomyces cerevisiae are structurally related dosage-dependent suppressors of metal toxicity. COT1 confers increased tolerance to high levels of cobalt; ZRC1 confers increased tolerance to high levels of zinc. The two genes are not linked and have been mapped; COT1 to chromosome XV and ZRC1 to chromosome XIII. Phenotypes related to metal homeostasis have been examined in strains with varied COT1 and ZRC1 gene doses. Overexpression of COT1 confers tolerance to moderately toxic levels of zinc and ZRC1 confers tolerance to moderately toxic levels of cobalt. Strains that carry null alleles at both loci are viable. The metal-hypersensitive phenotypes of mutations in either gene are largely unaffected by changes in dosage of the other. COT1 and ZRCI function independently in conferring tolerance to their respective metals, yet the uptake of cobalt ions by yeast cells is dependent on the gene dosage of ZRC1 as well as of COT1 Strains that overexpress ZRC1 have increased uptake of cobalt ions, while ZRCI null mutants exhibit decreased cobalt uptake. The defects in cobalt uptake due to mutations at COT1 and ZRC1 are additive, suggesting that the two genes are responsible for the majority of cobalt and zinc uptake in yeast cells. The function of either gene product seems to be more important in metal homeostasis than is the GRR1 gene product, which is also involved in metal metabolism. Mutations in the GRR1 gene have no effect on the cobalt-related phenotypes of strains that have altered gene dosage of either COT1 or ZRC1.
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    URL: http://dx.doi.org/10.1007/BF00285458
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    PDR3, a new yeast regulatory gene, is homologous toPDR1 and controls the multidrug resistance phenomenon (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 501-511 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcription factor ; Zinc finger ; Multidrug resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract TheSaccharomyces cerevisiae PDR3 gene, located near the centromere of chromosome II, has been completely sequenced and characterised. Mutationspdr3-1 andpdr3-2, which confer resistance to several antibiotics can be complemented by a wild-type allele of the PDR3 gene. The sequence of the wild-typePDR3 gene revealed the presence of a long open reading frame capable of encoding a 976-amino acid protein. The protein contains a single Zn(II)2Cys6 binuclear-type zinc finger homologous to the DNA-binding motifs of other transcriptional activators from lower eukaryotes. Evidence that the PDR3 protein is a transcriptional activator was provided by demonstrating that DNA-bound LexA-PDR3 fusion proteins stimulate expression of a nearby promoter containing LexA binding sites. The use of LexA-PDR3 fusions revealed that the protein contains two activation domains, one localised near the N-terminal, cysteine-rich domain and the other localised at the C-terminus. The salient feature of the PDR3 protein is its similarity to the protein coded byPDR1, a gene responsible forpleiotropicdrugresistance. The two proteins show 36% amino acid identity over their entire length and their zinc finger DNA-binding domains are highly conserved. The fact that the absence of both PDR1 and PDR3 (simultaneous disruption of the two genes) enhances multidrug sensitivity strongly suggests that the two transcriptional factors have closely related functions.
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    URL: http://dx.doi.org/10.1007/BF00583901
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    Two adjacent nuclear genes, ISF1 and NAM7/UPF1, cooperatively participate in mitochondrial functions in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 49-56 
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    ISSN: 1617-4623
    Keywords: Nuclear suppressor gene ; Mitochondrial functions ; Glucose repression ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We previously isolated a nuclear 5.7 kb genomic fragment carrying the NAM7/UPF1 gene, which is able to suppress mitochondrial splicing deficiency when present in multiple copies. We show here that an immediately adjacent gene ISF1 (Increasing Suppression Factor) increases the efficiency of the NAM7/UPF1 suppressor activity. The ISF1 gene has been independently isolated as the MBR3 gene and comparison of the ISF1 predicted protein sequence with data libraries revealed a significant similarity with the MBRI yeast protein. The ISF1 and NAM7 genes are transcribed in the same direction, and RNase mapping allowed the precise location of their termini within the intergenic region to be determined. The ISF1 gene is not essential for cell viability or respiratory growth. However as for many mitochondrial genes, ISF1 expression is sensitive to fermentative repression; in contrast expression of the NAM7 gene is unaffected by glucose. We propose that ISF1 could influence the NAM7/UPF1 function, possibly at the level of mRNA turnover, thus modulating the expression of nuclear genes involved in mitochondrial biogenesis.
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    Reduced but accurate translation from a mutant AUA initiation codon in the mitochondrial COX2 mRNA of Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 383-390 
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    ISSN: 1617-4623
    Keywords: Mitochondria ; Translation ; Yeast ; PET111 ; PET2858
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have changed the translation initiation codon of the COX2 mRNA of Saccharomyces cerevisiae from AUG to AUA, generating a mutation termed cox2-10. This mutation reduced translation of the COX2 mRNA at least five-fold without affecting the steady-state level of the mRNA, and produced a leaky nonrespiratory growth phenotype. To address the question of whether residual translation of the cox2-10 mRNA was initiating at the altered initiation codon or at the next AUG codon downstream (at position 14), we took advantage of the fact that the mature coxll protein is generated from the electrophoretically distinguishable coxII precursor by removal of the amino-terminal 15 residues, and that this processing can be blocked by a mutation in the nuclear gene PET2858. We constructed a pet2858, cox2-10 double mutant strain using a pet2858 allele from our mutant collection. The double mutant accumulated low levels of a polypeptide which comigrated with the coxII precursor protein, not the mature species, providing strong evidence that residual initiation was occurring at the mutant AUA codon. Residual translation of the mutant mRNA required the COX2 mRNA-specific activator PET111. Furthermore, growth of cox2-10 mutant strains was sensitive to alterations in PET111 gene dosage: the respiratory-defective growth phenotype was partially suppressed in haploid strains containing PET111 on a high-copy-number vector, but became more severe in diploid strains containing only one functional copy of PET111.
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    Characterization of the Saccharomyces cerevisiae nuclear gene CYB3 encoding a cytochrome b polypeptide of respiratory complex II (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 708-716 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Mitochondria ; Cytochrome b ; Complex II ; HAP2/3/4
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Computer-assisted structural analysis of the predicted product of the previously described open reading frame (ORF) YKL4 located on the left arm of chromosome XI of Saccharomyces cerevisiae revealed a high degree of similarity (〉50%) to bovine cytochrome b 560, the sdhC polypeptide of the Escherichia coli succinate dehydrogenase (SDH) complex and the protein specified by ORF137 located on the chloroplast DNA of Marchantia polymorpha. Disruption of the yeast gene severely impaired mitochondrial function, while Northern analysis showed it to be subject to catabolite repression. Deletion analysis of the CYB3 promoter identified a single HAP2/3/4-binding element that is necessary and sufficient for carbon source-dependent transcriptional regulation. These experiments also suggested the presence of additional, as yet unidentified, transcriptional control elements, both negative and positive. Taken together, these data lead us to conclude that the CYB3 gene encodes the yeast homolog of the bovine cytochrome b 560 component of complex II of the mitochondrial electron transport chain.
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    Functional analysis of the zinc cluster domain of the CYP1 (HAP1) complex regulator in heme-sufficient and heme-deficient yeast cells (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 699-707 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; CYP1(HAP1) protein ; Electron transport ; Oxygen and heme regulation ; Trans regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract CYP1 determines the expression of several genes whose transcription is heme-dependent in yeast. It exerts regulatory functions even in the absence of heme, usually considered to be its effector. It mediates both positive and negative effects, depending on the target gene and on the redox state of the cell. In the presence of heme, it binds through a cysteine-rich domain in which a histidine residue occupies the position of the sixth and essential cysteine of the otherwise classical zinc cluster DNA-binding domain exemplified by GAL4. We constructed specific missense mutations in the potential CYP1 zinc cluster domain by site-directed mutagenesis and looked for regulatory effects of the mutated proteins under specific physiological conditions. We show that CYP1 does belong to the zinc cluster regulatory family since a sixth essential cysteine residue is indeed present, albeit at a modified position when compared to the consensus sequence. We also show that the amino acid preceding the first cysteine residue of the DNA-binding domain critically affects the efficiency of regulation both in the presence and in the absence of heme: mutations known to affect DNA binding under heme-sufficient conditions also affect regulation under heme-deficient conditions. We therefore surmise that regulation under hemedeficient conditions is dependent upon DNA binding.
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    ACR1, a gene encoding a protein related to mitochondrial carriers, is essential for acetyl-CoA synthetase activity in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 727-735 
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    ISSN: 1617-4623
    Keywords: Acetyl-CoA synthetase ; Mitochondrial carriers ; Sequence ; Disruption ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The utilization of ethanol via acetate by the yeast Saccharomyces cerevisiae requires the presence of the enzyme acetyl-coenzyme A synthetase (acetyl-CoA synthetase), which catalyzes the activation of acetate to acetyl-coenzyme A (acetyl-CoA). We have isolated a mutant, termed acr1, defective for this activity by screening for mutants unable to utilize ethanol as a sole carbon source. Genetic and biochemical characterization show that, in this mutant, the structural gene for acetyl-CoA synthetase is not affected. Cloning and sequencing demonstrated that the ACR1 gene encodes a protein of 321 amino acids with a molecular mass of 35 370 Da. Computer analysis suggested that the ACR1 gene product (ACR1) is an integral membrane protein related to the family of mitochondrial carriers. The expression of the gene is induced by growing yeast cells in media containing ethanol or acetate as sole carbon sources and is repressed by glucose. ACR1 is essential for the utilization of ethanol and acetate since a mutant carrying a disruption in this gene is unable to grow on these compounds.
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    MBR1 and MBR3, two related yeast genes that can suppress the growth defect of hap2, hap3 and hap4 mutants (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 575-583 
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    ISSN: 1617-4623
    Keywords: Multicopy suppressors ; HAP2/3/4 activation complex ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two new yeast genes, named MBR1 and MBR3, were isolated as multicopy suppressors of the growth defect of a strain lacking the HAP2 transcriptional activator. Both genes when overexpressed can also suppress the growth defect of hap3 and hap4 null mutants. However, overexpression of MBRI cannot substitute for the HAP2/3/4 complex in activation of the CYC1 gene. Nucleotide sequencing of MBR1 and MBR3 revealed that these two genes encode serine-rich, hydrophilic proteins with regions of significant homology. The functional importance of one of these conserved regions was shown by mutagenesis. Disruption of MBR1 leads to a partial growth defect on glycerol medium. Disruption of MBR3 has no major effect but the double disruptant shows a synthetic phenotype suggesting that the MBR1 and MBR3 gene products participate in common function.
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    Identification of a sporulation-specific promoter regulating divergent transcription of two novel sporulation genes in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 661-672 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Meiosis Sporulation ; Divergent promoter ; Developmental regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Promoters that control gene expression in Saccharomyces cerevisiae only in a sporulation-specific manner have previously been isolated from a genomic yeast DNA library fused to a promoterless Escherichia coli lacZ gene. Two novel sporulation-specific genes, SPS18 and SPS19, were isolated using this technique. These genes are divergently controlled by the same promoter but with SPS18 expressed at four times the level of SPS19. Deletion analysis has shown that the promoter elements that exert sporulation control on each of the genes overlap, having a common 25 bp sequence located within the intergenic region. SPS18 encodes a 34-KDa protein of 300 amino acids that contains a putative zinc-binding domain and a region of highly basic residues that could target the protein to the nucleus. SPS19 encodes a 31-KDa protein of 295 amino acids, which has a peroxisomal targeting signal (SKL) at its C terminus; this protein belongs to the family of non-metallo short-chain alcohol dehydrogenases. A null mutation deleting the intergenic promoter prevented expression of both genes, and when homozygous in diploids, reduced the extent of sporulation four-fold; the spores that did form were viable, but failed to become resistant to ether, and were more sensitive to lytic enzymes. This phenotype reflects a defect in spore wall maturation, indicating that the product of at least one of the genes functions during the process of spore wall formation. Therefore these genes belong to the class of late sporulation-specific genes that are sequentially activated during the process of meiosis and spore formation.
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    In vivo analysis of chromatin following nystatin-mediated import of active enzymes into Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 100-104 
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    ISSN: 1617-4623
    Keywords: Chromatin ; Nystatin ; DNA topoisomerase I ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In vivo DNA-protein interactions are usually studied at the molecular level using DNA-degrading agents of low molecular weight. In order to be useful, macromolecular probes of chromatin structure, such as enzymes must first cross the cell membrane. In this paper we describe the introduction and evaluation of macromolecules with enzymatic activity into yeast spheroplasts treated with the polyene antibiotic nystatin. We report the low resolution analysis of chromatin structure in the promoter region of the Saccharomyces cerevisiae gene encoding DNA topoisomerase I by this technique using micrococcal nuclease and restriction enzymes.
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    Use of synthetic lethal mutants to clone and characterize a novel CTP synthetase gene in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 431-439 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Duplicate genes ; Synthetic lethal mutants ; CTP synthetase ; Pyrimidine biosynthetic pathway
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the pyrimidine biosynthetic pathway, CTP synthetase catalyses the conversion of uridine 5′-triphosphate (UTP) to cytidine 5′-triphosphate (CTP). In the yeast Saccharomyces cerevisiae, the URA7 gene encoding this enzyme was previously shown to be nonessential for cell viability. The present paper describes the selection of synthetic lethal mutants in the CTP biosynthetic pathway that led us to clone a second gene, named URA8, which also encodes a CTP synthetase. Comparison of the predicted amino acid sequences of the products of URA7 and URA8 shows 78% identity. Deletion of the URA8 gene is viable in a haploid strain but simultaneous presence of null alleles both URA7 and URA8 is lethal. Based on the codon bias values for the two genes and the intracellular concentrations of CTP in strains deleted for one of the two genes, relative to the wild-type level, URA7 appears to be the major gene for CTP biosynthesis. Nevertheless, URA8 alone also allows yeast growth, at least under standard laboratory conditions.
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    Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 517-527 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; HSP82 ; Random in vitro mutagenesis ; Temperature-sensitive mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The budding yeast Saccharomyces cerevisiae has two HSP90-related genes per haploid genome, HSP82 and HSC82. Random mutations were induced in vitro in the HSP82 gene by treatment of the plasmid with hydroxylamine. Four temperature-sensitive (ts) mutants and one simultaneously is and cold-sensitivie (cs) mutant were then selected in a yeast strain in which HSC82 had previously been disrupted. The mutants were found to have single base changes in the coding region, which caused single amino acid substitutions in the HSP82 protein. All of these mutations occurred in amino acid residues that are well conserved among HSP90-related proteins of various species from Escherichia coli to human. Various properties including cell morphology, macromolecular syntheses and thermosensitivity were examined in each mutant at both the permissive and nonpermissive temperatures. The mutations in HSP82 caused pleiotropic effects on these properties although the phenotypes exhibited at the nonpermissive temperature varied among the mutants.
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    The hypo-osmolarity-sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of β-glucanase (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 641-648 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell wall ; Protein kinase C ; β-Glucanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To obtain more information about the cell wall organization of Saccharomyces cerevisiae, we have developed a novel screening system to obtain cell wall-defective mutants, using a density gradient centrifugation method. Nine hypo-osmolarity-sensitive mutants were classified into two complementation groups, hpo1 and hpo2. Phase contrast microscopic observation showed that mutant cells bearing lesions at either locus became abnormally large. A gene that complemented the mutant phenotype of hpo2 was cloned and sequenced. This gene turned out to be identical to PKC1, which encodes the yeast homologue of mammalian protein kinase C. Complementation tests with pkc1Δ showed that hpo2 is allelic to pkc1. To study the reason for the fragility of hpo2 cells, cell wall was isolated and the glucan was analyzed. The amount of alkali, acid-insoluble glucan, which is responsible for the rigidity of the cell wall, was reduced to about 30% that of the wild-type cell and this may be the major cause of the fragility of the hpo2 mutant cell. Analysis of total wall proteins in hpo2 mutant cells on SDS-polyacrylamide gels revealed that a 33 kDa protein was overproduced two- to threefold relative to the wild-type level. This 33 kDa protein was identified as a β-glucanase, encoded by BGL2. Disruption of BGL2 in the hpo2 mutant partially rescued the growth rate defect. This suggests that the PKC1 kinase cascade regulates BGL2 expression negatively and overproduction of the β-glucanase is partially responsible for the growth defect. Since the bgl2 disruption did not rescue the hypo-osmolarty-sensitive phenotype of the hpo2 mutant, PKC1 must negatively regulate other enzymes involved in the biosynthesis and metabolism of the cell wall.
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    Polyubiquitin gene expression contributes to oxidative stress resistance in respiratory yeast (Saccharomyces cerevisiae) (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 358-362 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Oxidative stress ; High temperature viability ; Ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract UBI4, the polyubiquitin gene of Saccharomyces cerevisiae, is expressed at a low level in vegetative cells, yet induced strongly in response to starvation, cadmium, DNA-damaging agents and heat shock. UBI4 is also expressed at a higher basal level in cells growing by respiration as compared to glucose-repressed cells growing by fermentation. This higher UBI4 expression of respiratory cultures probably helps to counteract the greater oxidative stress of respiratory growth. The effects of inactivating UBI4 on high temperature viability are more marked with respiratory cultures. Also loss of UBI4 leads to a considerably increased rate of killing of respiring cells by hydrogen peroxide, whereas the same gene inactivation has relatively little effect on the peroxide sensitivity of cells in which mitochondrial functions are repressed. This is the first study to reveal that ubiquitin levels in cells can influence their ability to withstand oxidative stress.
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    Open reading frames in the antisense strands of genes coding for glycolytic enzymes in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 363-368 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Glycolysis ; Phosphoglucose isomerase ; Antisense ; Double-strand coding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Open reading frames longer than 300 bases were observed in the antisense strands of the genes coding for the glycolytic enzymes phosphoglucose isomerase, phosphoglycerate mutase, pyruvate kinase and alcohol dehydrogenase I. The open reading frames on both strands are in codon register. It has been suggested that proteins coded in codon register by complementary DNA strands can bind to each other. Consequently, it was interesting to investigate whether the open reading frames in the antisense strands of glycolytic enzyme genes are functional. We used oligonucleotide-directed mutagenesis of the PGI1 phosphoglucose isomerase gene to introduce pairs of closely spaced base substitutions that resulted in stop codons in one strand and only silent replacements in the other. Introduction of the two stop codons into the PGI1 sense strand caused the same physiological defects as already observed for pgi1 deletion mutants. No detectable effects were caused by the two stop codons in the antisense strand. A deletion that removed a section from − 31 by to + 109 by of the PGI1 gene but left 83 bases of the 3′ region beyond the antisense open reading frame had the same phenotype as a deletion removing both reading frames. A similar pair of deletions of the PYK1 gene and its antisense reading frame showed identical defects. Our own Northern experiments and those reported by other authors using double-stranded probes detected only one transcript for each gene. These observations indicate that the antisense reading frames are not functional. On the other hand, evidence is provided to show that the rather long reading frames in the antisense strands of these glycolytic enzyme genes could arise from the strongly selective codon usage in highly expressed yeast genes, which reduces the frequency of stop codons in the antisense strand.
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    Meiosis-dependent tyrosine phosphorylation of a yeast protein related to the mouse p51ferT (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 160-167 
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    ISSN: 1617-4623
    Keywords: p51ferT ; Yeast ; Meiosis ; Phosphotyrosine Kinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The FER locus of the mouse encodes two mRNA species: one is constitutively transcribed, giving rise to a 94 kDa tyrosine kinase (p94ferT); the second is a meiosis-specific RNA that gives rise to a 51 kDa tyrosine kinase (p51ferT). The p51ferT RNA and protein accumulate in primary spermatocytes that are in prophase of the first meiotic division. By using polyclonal antibodies directed against synthetic peptides derived from the unique amino-terminus of the mouse p51ferT, a 51 kDa phosphotyrosyl protein — p51y — was identified in Saccharomyces cerevisiae. The p51y protein is constitutively expressed in yeast, but in meiotic cells, concomitantly with commitment to meiotic recombination, its level of phosphorylation on tyrosine residues is increased. A different pattern of phosphorylation is observed on serine residues: at early meiotic times the level is decreased, while in later meiotic time the level increases, reaching the vegetative level. When p51ferT is ectopically expressed in yeast, it is active, leading to preferential phosphorylation of an approx. 65 kDa protein. A similar pattern of phosphorylation by p51ferT is seen in mammalian cells.
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    The archaebacterial membrane protein bacterio-opsin is expressed and N-terminally processed in the yeast Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 183-188 
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    ISSN: 1617-4623
    Keywords: Bacterio-opsin ; Expression ; Yeast ; Saccharomyces cerevisiae ; Membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The bop gene codes for the membrane protein bacterio-opsin (BO), which on binding all-trans-retinal, constitutes the light-driven proton pump bacteriorhodopsin (BR) in the archaebacterium Halobacterium salinarium The designation H. salinarium instead of the former designation H. halobium is used throughout this paper following the classification of Tindall (1992) . This gene was cloned in a yeast multi-copy vector and expressed in Saccharomyces cerevisiae under the control of the constitutive ADH1 promoter. Both the authentic gene and a modified form lacking the precursor sequence were expressed in yeast. Both proteins are incorporated into the membrane in S. cerevisiae. The presequence is thus not required for membrane targeting and insertion of the archaebacterial protein in budding yeast, or in the fission yeast Schizosaccharomyces pombe, as has been shown previously. However, in contrast to S. pombe transformants, which take on a reddish colour when all-trans-retinal is added to the culture medium as a result of the in vivo regeneration of the pigment, S. cerevisiae cells expressing BO do not take on a red colour. The precursor of BO is processed to a protein identical in size to the mature BO found in the purple membrane of Halobacterium. The efficiency of processing in S. cerevisiae is dependent on growth phase, as well as on the composition of the medium and on the strain used. The efficiency of processing of BR is reduced in S. pombe and in a retinal-deficient strain of H. salinarium, when retinal is present in the medium.
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    Heterospecific cloning of Arabidopsis thaliana cDNAs by direct complementation of pyrimidine auxotrophic mutants of Saccharomyces cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the second, fifth and sixth steps of the de novo pyrimidine biosynthesis pathway (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 23-32 
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    ISSN: 1617-4623
    Keywords: Arabidopsis thaliana ; Saccharomyces cerevisiae ; Complementation ; Aspartate transcarbamylase ; Orotate phosphoribosyl transferase ; Orotidine-5′-phosphate decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An Arabidopsis thaliana cDNA library was used to complement Saccharomyces cerevisiae pyrimidine auxotrophic mutants. Mutants in all but one (carbamylphosphate synthetase) of the six steps in the de novo pyrimidine biosynthetic pathway could be complemented. We report here the cloning, sequencing and computer analysis of two cDNAs encoding the aspartate transcarbamylase (ATCase; EC 2.1.3.2) and orotate phosphoribosyltransferase-orotidine-5′-phosphate decarboxylase (OPRTase-OMP-decase; EC 2.4.2.10, EC 4.1.1.23) enzymes. These results confirm the presence in A. thaliana of a bifunctional gene whose product catalyses the last two steps of the pyrimidine biosynthetic pathway, as previously suggested by biochemical studies. The ATCase encoding cDNA sequence (PYRB gene) shows an open reading frame (ORF) of 1173 by coding for 390 amino acids. The cDNA encoding OPRTase-OMPdecase (PYRE-F gene) shows an ORF of 1431 by coding for 476 amino acids. Computer analysis of the deduced amino acid sequences of both cDNAs shows the expected high similarity with the ATCase, ornithine transcarbamylase (OTCase; EC 2.1.3.3), OPRTase and OMPdecase families. This heterospecific cloning approach increases our understanding of the genetic organization and interspecific functional conservation of the pyrimidine biosynthetic pathway and underlines its usefulness as a model for evolutionary studies.
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    Sequence of the HAP3 transcription factor of Kluyveromyces lactis predicts the presence of a novel 4-cysteine zinc-finger motif (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 96-106 
    Details
    ISSN: 1617-4623
    Keywords: HAP3 ; Saccharomyces cerevisiae ; Kluyveromyces lactis ; Zinc finger ; Carbon source regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Kluyveromyces lactis homologue of the Saccharomyces cerevisiae HAP3 gene was isolated by functional complementation of the respiratory-deficient phenotype of the S. cerevisiae hap3::HIS4 strain SHY40. The KlHAP3 gene encodes a protein of 205 amino acids, of which the central B-domain of 90 residues is highly homologous to HAP3 counterparts of S. cerevisiae and higher eukaryotes. The protein contains a novel 4-cysteine zinc-finger motif and we propose by analogy that all other homologous HAP3 proteins contain the same motif, with the position containing the third cysteine being occupied by a serine residue. In contrast to the situation in S. cerevisiae, disruption of the KlHAP3 gene in K. lactis does not result in a respiratory-deficient phenotype and the growth of the null strain is indistinguishable from wild type. There is also no effect on the expression of the carbon source-regulated KlCYC1 gene, suggesting either a different role for the HAP2/3/4 complex, or the existence of a different mechanism of carbon source regulation. Sequence verification of the S. cerevisiae HAP3 locus reveals that, just as in K. lactis, a long open reading frame (ORF) is present upstream of the HAP3 gene. These highly homologous ORFs are predicted to have at least eight membrane-spanning fragments, but do not show significant homology to any known sequence present in databases. The ScORFX gene is transcribed in the opposite direction to ScHAP3, but, in contrast to an earlier report by Hahn et al. (1988), the transcripts of the two genes do not overlap. The model proposed by these authors, in which the ScHAP3 gene is regulated by an anti-sense non-coding mRNA, is therefore not correct.
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    URL: http://dx.doi.org/10.1007/BF00279755
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    Expression of human poly(ADP-ribose) polymerase in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 686-693 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Saccharomyces cerevisiae ; Poly(ADP-ribose) polymerase ; DNA repair
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The coding sequence for human poly(ADP-ribose) polymerase was expressed inducibly in Saccharomyces cerevisiae from a low-copy-number plasmid vector. Cell free extracts of induced cells had poly(ADPribose) polymerase activity when assayed under standard conditions; activity could not be detected in non-induced cell extracts. Induced cells formed poly(ADP-ribose) in vivo, and levels of these polymers increased when cells were treated with the alkylating agent N-methyl-N′-nitro-N-nitrosoguanidine (MNNG). The cytotoxicity of this agent was increased in induced cells, and in vivo labelling with [3H]adenine further decreased their viability. Increased levels of poly(ADP-ribose) found in cells treated with the alkylating agent were not accompanied by lowering of the NAD concentration.
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    A new yeast gene, HTR1, required for growth at high temperature, is needed for recovery from mating pheromone-induced G1 arrest (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 107-116 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; ts mutant ; Recovery ; HTR1 ; MCS1/SSD1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A new temperature-sensitive mutant of Saccharomyces cerevisiae was isolated. Arrested cells grown at the nonpermissive temperature were of dumb-bell shape and contained large vacuoles. A DNA fragment was cloned based on its ability to complement this temperature sensitivity. The HTR1 gene encodes a putative protein of 93 kDa without significant homology to any known proteins. The gene was mapped between ade5 and lys5 on the left arm of chromosome VII. The phenotype of the gene disruptant appeared to be strain-specific; disruption of the gene in strain W303 caused the cells to become temperature sensitive. The arrested phenotype here was similar to that of the original is mutant and cells in G2/M phase predominated at high temperature. Another disruptant in a strain YPH background grew slowly at high temperature due to slow progression through G2/M phase, and morphologically abnormal (elongated) cells accumulated. A single-copy suppressor that alleviated the temperature-sensitive defects in both strains was identified as MCS1/SSD1. The wild-type strains W303 and YPH are known to carry defective MCS1/SSD1 alleles; hence HTR1 may function redundantly with MCS1/SSD1 to suppress the temperature-sensitive phenotypes. In addition, based on a halo bioassay, the disruptant strains appeared to be defective in recovery from, or adaptive response to G1 arrest mediated by mating pheromone, even at the permissive temperature. Thus the gene has at least two functions and is designated HTR1 (required for high temperature growth and recovery from G1 arrest induced by mating pheromone).
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    Two subclasses of guanine exchange factor (GEF) domains revealed by comparison of activities of chimeric genes constructed from CDC25, SDC25 and BUD5 in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 167-176 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell cycle ; Bud site selection ; Guanine exchange factor ; Ras
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Guanine Exchange Factor (GEF) activity for Ras proteins has been associated with a conserved domain in Cdc25p, Sdc25p in Saccharomyces cerevisiae and several other proteins recently found in other eukaryotes. We have assessed the structure-function relationships between three different members of this family in S. cerevisiae, Cdc25p, Sdc25p and Bud5p. Cdc25p controls the Ras pathway, whereas Bud5p controls bud site localization. We demonstrate that the GEF domain of Sdc25p is closely related to that of Cdc25p. We first constructed a thermosensitive allele of SDC25 by specifically altering amino acid positions known to be changed in the cdc25-1 mutation. Secondly, we constructed three chimeric genes from CDC25 and SDC25, the products of which are as active in the Ras pathway as are the wild-type proteins. In contrast, similar chimeras made between CDC25 and BUD5 lead to proteins that are inactive both in the Ras and budding control pathways. This difference in the ability of chimeric proteins to retain activity allows us to define two subclasses of structurally different GEFs: Cdc25p and Sdc25p are Ras-specific GEFs, and Bud5p is a putative GEF for the Rsr1/Bud1 Rap-like protein.
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    Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to rna14 mutations (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 323-333 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; mRNA decay Poly(A) tail ; Ty transposition ; SSM4 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Decay rates of mRNAs depend on many elements and among these, the role of the poly(A) tail is now well established. In the yeast Saccharomyces cerevisiae, thermosensitive mutations in two genes, RNA14 and RNA15, result in mRNAs having shorter poly(A) tails and reduced half-life. To identify other components interacting in the same process, we have used a genetic approach to isolate mutations that suppress the thermosensitivity of an rna14 mutant strain. Mutations in a single locus, named SSM4, not only suppress the cell growth phenotype but also the mRNA instability and extend the short mRNA poly(A) tails. The frequency of appearance and the recessive nature of these mutations suggested that the suppressor effect was probably due to a loss of function. We failed to clone the SSM4 gene directly by complementation, owing to its absence from gene banks; it later emerged that the gene is toxic to Escherichia coli, but we have nevertheless been able to clone the SSM4 sequence by Ty element transposition tagging. Disruption of the SSM4 gene does not affect cell viability and suppresses the rna14 mutant phenotypes. The protein encoded by the SSM4 gene has a calculated molecular mass of 151 kDa and does not contain any known motif or show homology with known proteins. The toxicity of the SSM4 gene in E. coli suggests that a direct biochemical activity is associated with the corresponding protein.
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    Genetic interactions between SIN3 mutations and the Saccharomyces cerevisiae transcriptional activators encoded by MCM1, STE12, and SWI1 (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 675-685 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Transcriptional regulation ; SIN3 STE12 ; SWI1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract SIN3 was first identified by a mutation which suppresses the effects of an swi5 mutation on expression of the HO gene in Saccharomyces cerevisiae. We now show that a sin3 mutation also partially suppresses the effects of swi1 on HO transcription, and partially suppresses the growth defect and inositol requirement observed in swi1 mutants. This suggests that SIN3 and SWI1 may play opposite regulatory roles in controlling expression of many yeast genes. Yeast SIN3 has been shown to function as a negative transcriptional regulator of a number of yeast genes. However, expression of the yeast STE6 gene is reduced in a sin3 mutant strain. This suggests that SIN3 functions as a positive regulator for STE6 transcription, although this apparent activation function could be indirect. In order to understand how SIN3 functions in STE6 regulation, we have performed a genetic analysis. It has been previously demonstrated that MCM1 and STE12 are transcriptional activators of a-specific genes such as STE6, and we now show that SWI1 is also required for STE6 expression. Our data suggest that STE12 and SWI1 function in different pathways of activation, and that STE12 is epistatic to SIN3 and SWI1. We show that the activities of the Mcmlp and Stel2p activators are modestly reduced in a sin3 mutant strain, and that phosphorylation of the Stel2p activator is decreased in a sin3 mutant. Thus, it is possible that the decreased transcription of STE6 in sin3 mutants is due to the combined effect of the diminished activities of Mcmlp and Stel2p.
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    Genetic interaction between the Ras-CAMP pathway and the Dis2s1/Glc7 protein phosphatase in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 257-262 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Protein phosphatase ; Ras-cAMP pathway ; DIS2S1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae DIS2S1/GLC7 gene encodes a type 1 protein phosphatase indispensable for cell proliferation. We found that introduction of a multicopy DIS2S1 plasmid impaired growth of cells with reduced activity of the cAMP-dependent protein kinase. In order to understand further the interaction between the two enzymes, a temperature-sensitive mutation in the DIS2S1 gene was isolated. The mutant accumulated less glycogen than wild type at the permissive temperature, indicating that activity of the Dis2s1 protein phosphatase is attenuated by the mutation. Furthermore, the dis2s1 ts mutation was shown to be suppressed by a multicopy plasmid harboring PDE2, a gene for cAMP phosphodiesterase. These results indicate that the Ras-cAMP pathway interacts genetically with the DIS2S1/GLC7 gene.
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    URL: http://dx.doi.org/10.1007/BF00280414
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    Stress-induced transcriptional activation mediated by YAP1 and YAP2 genes that encode the Jun family of transcriptional activators in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 250-256 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcriptional activator ; AP-1 ; Stress response
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae YAP2 gene encoding an AP-1-like transcriptional activator protein was cloned by selection for genes that confer pleiotropic drug resistance when present in high copy number. The novel YAP2 gene encodes a protein of 45827 daltons and is homologous in part to a known transcriptional activator protein encoded by YAP1/PDR4/SNQ3/PAR1. Homology was found only in both terminal regions. The N-terminal portion contains a region rich in basic amino acids, followed by a “leucine zipper” motif. Overexpression of YAP2 led to the induction of expression of an AP-1 recognition element (ARE)-dependent promoter. The yap1 disruptant has been shown to be sensitive to H2O2. In this study, we demonstrated that the yap1 disruptant is also unable to grow in medium containing 150 μM cadmium, whereas the yap2 disruptant exhibited no significant phenotypes. However, YAP2 in high copy number did suppress cadmium sensitivity, but not H2O2 sensitivity of the yap1 disruptant. YAP1 was able to mediate both cadmium- and H2O2-induced transcriptional activation of an ARE-dependent promoter. A high-copy-number plasmid bearing YAP2 mediated cadmium-induced transcriptional activation of this promoter. The inductions were prevented by the antioxidant N-acetyl-l-cysteine.
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    The 3′ → 5′ exonucleases of both DNA polymerases δ and ε participate in correcting errors of DNA replication in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 289-296 
    Details
    ISSN: 1617-4623
    Keywords: DNA polymerases ε and δ ; 3′ → 5′ Exonuclease ; Replication errors ; Spontaneous mutations ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract DNA polymerases II (ε) and III(δ) are the only nuclear DNA polymerases known to possess an intrinsic 3′ → 5′ exonuclease in Saccharomyces cerevisiae. We have investigated the spontaneous mutator phenotypes of DNA polymerase δ and ε 3′ → 5′ exonuclease-deficient mutants, pol3-01 and pol2-4, respectively. pol3-01 and pol2-4 increased spontaneous mutation rates by factors of the order of 102 and 101, respectively, measured as URA3 forward mutation and his7-2 reversion. Surprisingly, a double mutant pol2-4 pol3-01 haploid was inviable. This was probably due to accumulation of unedited errors, since a pol2-4/pol2-4 pol3-01/pol3-01 diploid was viable, with the spontaneous his7-2 reversion rate increased by about 2 × 103-fold. Analysis of mutation rates of double mutants indicated that the 3′ → 5′ exonucleases of DNA polymerases δ and ε can act competitively and that, like the 3′ → 5′ exonuclease of DNA polymerase δ the 3′ → 5′ exonuclease of DNA polymerase ε acts in series with the PMS1 mismatch correction system. Mutational spectra at a URA3 gene placed in both orientations near to a defined replication origin provided evidence that the 3′ → 5′ exonucleases of DNA polymerases δ and ε act on opposite DNA strands, but were in sufficient to distinguish conclusively between different models of DNA replication.
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    A novel method for efficient expression cloning of fungal enzyme genes (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 253-260 
    Details
    ISSN: 1617-4623
    Keywords: Recombinant DNA ; Saccharomyces cerevisiae ; Endo-β-glucanase ; Endo-xylanase ; Heterologous expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have developed a method for fast and efficient isolation of enzyme genes from filamentous fungi by combining the ability of Saccharomyces cerevisiae to express heterologous genes with the utilisation of sensitive and reliable enzyme assays. A cDNA library from the fungus Humicola insolens was constructed in a S. cerevisiae/Escherichia coli shuttle vector in E. coli. Sub-pools of the library were subsequently screened for enzyme activity in S. cerevisiae. More than 130 clones were identified as positive in either an endo-β-glucanase or an endo-xylanase assay. Based on a partial characterization of the DNA sequence of the individual clones, they could be grouped into five distinct types of endo-β-glucanases and three types of endo-xylanases. A representative cDNA from each type was sub-cloned in an Aspergillus vector and expressed in A. oryzae. The new cloning method may be an important alternative to traditional cloning methods based on amino acid sequence information.
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    Efficient UV stimulation of yeast integrative transformation requires damage on both plasmid strands (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 308-314 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Integrative plasmids ; Recombinational structures ; UV irradiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nature of UV-induced pre-recombinational structures was studied using transformation of Saccharomyces cerevisiae cells with non-replicative plasmids. Transformation by double-stranded plasmids irradiated with UV was stimulated up to 50-fold, and both plasmid integration and conversion of the mutated chromosomal selective gene were found to be equally increased. The stimulation observed with such ‘totally’ irradiated plasmids was not found with plasmids bearing lesions in only one strand. This effect is attributed to the formation by excision repair of recombinogenic structures consisting of a pyrimidine dimer opposite a gap. When single-stranded integrative plasmids were irradiated, their transforming potential was decreased but the proportion of transformants that arose by gene conversion, rather than by plasmid integration, was increased from 8% to 49% as a function of the UV dose. Possible reasons why single-strand UV lesions favour gene conversion are discussed.
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    Pleiotropic function of ArgRIIIp (Arg82p), one of the regulators of arginine metabolism in Saccharomyces cerevisiae. Role in expression of cell-type-specific genes (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 315-324 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Arginine ; Cell-type regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract ArgRIIIp (Arg82p), together with ArgRIp (Arg80p), ArgRIIp (Arg81p) and Mcmlp, regulates the expression of arginine anabolic and catabolic genes. An argRIII mutant constitutively expresses five anabolic enzymes and is impaired in the induction of the synthesis of two catabolic enzymes. A genomic disruption of the ARGRIII gene not only leads to an argR phenotype, but also prevents cell growth at 37°C. The disrupted strain is sterile especially in an α background and transcription of α- and a-specific genes (MFα1 and STE2) is strongly reduced. By gel retardation assays we show that the binding of the Mcmlp present in a crude protein extract from an argRIII mutant strain to the P(PAL) sequence is impaired. Sporulation of α/a argRIII:: URA3 homozygous diploids is also affected. Overexpression of Mcm1p in an argRIII-disrupted strain restores the mating competence of the strain, the ability to form a protein complex with P(PAL) DNA in vitro, and the regulation of arginine metabolism. However, overexpression of Mcm1p does not complement the sporulation deficiency of the argRIII-disrupted strain, nor does it complement its growth defect at 37°C. Western blot analysis indicates that Mcm1p is less abundant in a strain devoid of ArgRIIIp than in wild type.
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    Shared control of maltose induction and catabolite repression of the MAL structural genes in Saccharomyces (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 622-630 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Yeast Catabolite repression ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Maltose utilization in yeast requires the presence of any one of the five unlinked, homologous MAL loci. Transcription of the two structural genes MALT (permease) and MALS (maltase) is induced by maltose and catabolite-repressed by glucose. MAL6T and MAL6S share a common 5′ intergenic sequence; deletion studies within this sequence revealed a bi-directionally functioning upstream activation sequence (UASM) consisting of four 11bp homologous sites. Activation of these sites by the MALR protein results in the coordinate expression of MAL6T and MAL6S. The basal promoter activates MALS expression to a greater extent than MALT and is located in a region that overlaps UASM. Deletion of several subsites within the UASM has an asymmetric effect on MAL gene expression, having a greater affect on MALT than on MALS. Catabolite repression of MAL6T and MAL6S by glucose is controlled at several levels. Using disruption mutants, the positively acting MAL1R protein was also found to play a role in catabolite repression of MAL6T and MAL6S.
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    RPK1, an essential yeast protein kinase involved in the regulation of the onset of mitosis, shows homology to mammalian dual-specificity kinases (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 641-653 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; RPK1 gene ; Protein kinase ; DNA replication ; Initiation of mitosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We report here the sequence of RPK1 (for Regulatory cell Proliferation Kinase), a new Saccharomyces cerevisiae gene coding for a protein with sequence similarities to serine/threonine protein kinases. The protein sequence of 764 amino acids includes an amino-terminal domain (residues 1–410), which may be involved in regulation of the kinase domain (residues 411–764). The catalytic domain of Rpkl is not closely related to other known yeast protein kinases but exhibits strong homology to a newly discovered group of mammalian kinases (PYT, TTK, esk) with serine/threonine/tyrosine kinase activity. Null alleles of RPK1 are lethal and thus this gene belongs to the small group of yeast protein kinase genes that are essential for cell growth. In addition, eliminating the expression of RPK1 gives rise to the accumulation of non-viable cells with less than a 1 N DNA content suggesting that cells proceed into mitosis without completion of DNA synthesis. Therefore, the Rpkt kinase may function in a checkpoint control which couples DNA replication to mitosis. The level of the RPK1 transcript is extremely low and constant throughout the mitotic cycle. However it is regulated during cellular differentiation, being decreased in α-factor-treated a cells and increased late in meiosis in a/α diploids. Taken together, our results suggest that Rpk1 is involved in a pathway that coordinates cell proliferation and differentiation.
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    Studies on the activity ofKluyveromyces lactis S-adenosylmethionine: Δ 24-sterol methyltransferase in presence of polyenic antifungal agents (1994)
    Springer
    Mycopathologia 126 (1994), S. 75-83 
    Details
    ISSN: 1573-0832
    Keywords: Ergosterol synthesis ; Polyenic antifungal agents ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The S-adenosylmethionine: Δ 24-sterol methyltransferase (24 SMT) primarily considered as a mitochondrial enzyme, was recently mainly detected in lipid particles of yeasts. It catalyses the methylation of zymosterol which is an essential reaction for the synthesis of ergosterol. We have investigated in cellular extracts of twoKluyveromyces lactis strains the action of polyenic antifungal agents on the activity of this enzyme. Low concentrations of amphotericin B, candicidin and pimaricin strongly stimulate this activity, while high concentrations inhibit it or have no effect. Whatever the doses used, nystatin and filipin had no significant influence on this activity. According to the molar ratio amphotericin B/total sterols of the enzyme preparation, the interference of amphotericin B on the 24 SMT activity may result of two mechanisms.
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    Lysine inhibition of Saccharomyces cerevisiae: role of repressible L-lysine ε-aminotransferase (1994)
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 572-575 
    Details
    ISSN: 1573-0972
    Keywords: Growth inhibition ; L-lysine ε-aminotransferase ; nitrogen limitation ; α-oxoadipic acid ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Lysine added to grain mashes under nitrogen-limiting conditions (as in most industrial fermentations) inhibited growth of Saccharomyces cerevisiae. This inhibition was relieved by raising the assimilable nitrogen content. Lysine-induced inhibition is not mediated through accumulation of α-oxoadipic acid, an intermediate of lysine metabolism which accumulates by a back up of intermediates in de novo synthesis. Lysine degradation is regulated by the synthesis of L-lysine ε-aminotransferase, an enzyme that catalyses the first step in one of three possible routes of lysine degradation (not previously reported in S. cerevisiae). Synthesis is repressed under nitrogenlimiting conditions, but derepressed when excess assimilable nitrogen is available. Derepression results in degradation of lysine and decreases inhibitory effects on growth. The toxic compound appears to be lysine itself.
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    The glycerol kinase (GUT1) gene of Saccharomyces cerevisiae: cloning and characterization (1993)
    Springer
    Current genetics 24 (1993), S. 21-25 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Glycerol kinase ; GUT1 ; ADR1 control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The GUT1 gene of Saccharomyces cerevisiae, encoding glycerol kinase, was cloned and sequenced. The cloned genomic DNA fragment contains an open reading frame potentially coding for a protein of 709 amino acids with homology to bacterial glycerol kinases (40.8% identity over 502 amino acids, and 42.1% identity over 496 amino acids, in comparison to the smaller E. coli and B. subtilis enzymes). Disruption of GUT1 showed that the gene is required for growth on glycerol, but not on glucose or ethanol media. No glycerol kinase activity was detected in the disruption mutant. According to enzyme activity and transcript analysis, synthesis of glycerol kinase is repressed by glucose, and derepression is ADR1-dependent.
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    ‘Phase variation’-type regulation of gene expression and gene replacement mediated by FLP recombinase in the yeast Saccharomyces cerevisiae (1993)
    Springer
    Current genetics 24 (1993), S. 26-31 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; FLP ; Phase variation-type expression ; Gene replacement
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Expression of a neomycin phosphotransferase II (NPTII) gene has been designed to be regulated by an FLP-mediated switching of the orientation of the NPTII coding region located on the invertible DNA segment in episomal yeast plasmids. Inversion of the segment from inverted to direct orientation with respect to the promoter resulted in a dramatic increase in G418 resistance. FLP also promoted a double reciprocal exchange between the transforming and the resident 2-μm plasmid, leading to insertion of the FLP and REP2 genes into the transforming plasmid. The results demonstrate a possible use of FLP recombinase for ‘phase variation’-type regulation of gene expression and gene replacement in eukaryotic cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00324661
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  • 96
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    Cloning and expression of Hormoconis resinae glucoamylase P cDNA in Saccharomyces cerevisiae (1993)
    Springer
    Current genetics 24 (1993), S. 38-44 
    Details
    ISSN: 1432-0983
    Keywords: Glucoamylase ; Gene cloning ; Hormoconis resinae ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA coding for glucoamylase P of Hormoconis resinae was cloned using a synthetic oligonucleotide probe coding for a peptide fragment of the purified enzyme and polyclonal anti-glucoamylase antibodies. Nucleotide-sequence analysis revealed an open reading frame of 1848 base pairs coding for a protein of 616 amino-acid residues. Comparison with other fungal glucoamylase amino-acid sequences showed homologies of 37–48%. The glucoamylase cDNA, when introduced into Saccharomyces cerevisiae under the control of the yeast ADC1 promoter, directed the secretion of active glucoamylase P into the growth medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00324663
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  • 97
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    Normal mitochondrial structure and genome maintenance in yeast requires the dynamin-like product of the MGM1 gene (1993)
    Springer
    Current genetics 24 (1993), S. 141-148 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Dynamin ; Mitochondria ; GTP binding protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The isolation and characterization of MGM1, and yeast gene with homology to members of the dynamin gene family, is described. The MGM1 gene is located on the right arm of chromosome XV between STE4 and PTP2. Sequence analysis revealed a single open reading frame of 902 residues capable of encoding a protein with an approximate molecular mass of 101 kDa. Loss of MGM1 resulted in slow growth on rich medium, failure to grow on non-fermentable carbon sources, and loss of mitochondrial DNA. The mitochondria also appeared abnormal when visualized with an antibody to a mitochondrial-matrix marker. MGM1 encodes a dynamin-like protein involved in the propagation of functional mitochondria in yeast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00324678
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  • 98
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    Characterization of a second nuclear gene, AEP1, required for expression of the mitochondrial OLI1 gene in Saccharomyces cerevisiae (1993)
    Springer
    Current genetics 24 (1993), S. 126-135 
    Details
    ISSN: 1432-0983
    Keywords: AEP1 ; Yeast ; Mitochindria ; ATP synthase ; PET gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Due to mutation in a single nuclear locus, AEP1, the temperature-conditional pet mutant ts1860 of Saccharomyces cerevisiae fails to synthesize mitochondrial ATP synthase subunit 9 at the restrictive temperature of 36°C. The presence at this temperature of near-normal levels of the cognate oli1 mRNA in mutant ts1860 indicates that, as previously shown, the product of the AEP1 gene is required for translation of the mitochondrial oli1 transcript. In this study the AEP1 gene has been cloned from a wild-type yeast genomic library by genetic complementation of a temperature-conditional aep1 strain at the restrictive temperature. A 2,330-bp genomic fragment which restores subunit 9 synthesis in aep1 mutant strains was characterized. This fragment encoded five open reading frames: the longest of these, at 1,554 nucleotides, was identified as the AEP1 gene, since disruption of this reading frame generated a non-conditional pet strain unable to synthesize subunit 9. The predicted product of AEP1 is a basic, hydrophilic protein of 59,571 Da which possesses a putative mitochondrial address sequence. Hybridization studies with AEP1-specific probes indicate that the gene is located on chromosome XIII and produces several poly(A)+ transcripts ranging in size from 0.9 to 2.7 kb. None of the identified reading frames share significant homologies with entries of several data bases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00324676
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  • 99
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    Electronic Resource
    Reorientation of the distal region in linkage group IIR of fission yeast (1993)
    Springer
    Current genetics 24 (1993), S. 179-180 
    Details
    ISSN: 1432-0983
    Keywords: Mapping ; Yeast ; Schizosaccharomyces pombe
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genetic map of the fission yeast Schizosaccharomyces pombe has been revised in the distal region of chromosome arm IIR. The spo4 locus, hitherto considered the outermost marker, has been moved to an intermediate position. As a result, and in accordance with recent physical mapping data, the order of the entire distal subgroup of some 12 genetic markers is reversed relative to previously published gene maps.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00324684
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  • 100
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    Molecular cloning of the PEL1 gene of Saccharomyces cerevisiae that is essential for the viability of petite mutants (1993)
    Springer
    Current genetics 24 (1993), S. 307-312 
    Details
    ISSN: 1432-0983
    Keywords: Growth control ; Genetic mapping ; Molecular cloning ; Nucleo-mitochondrial interaction ; Saccharomyces cerevisiae ; Viability of petites
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The PEL1 gene of Saccharomyces cerevisiae is essential for the cell viability of mitochondrial petite mutants, for the ability to utilize glycerol and ethanol on synthetic medium, and for cell growth at higher temperatures. By tetrad analysis the gene was assigned to chromosome III, centromere proximal of LEU2. The PEL1 gene has been isolated and cloned by the complementation of a pel1 mutation. The molecular analysis of the chromosomal insert carrying PEL1 revealed that this gene corresponds to the YCL4W open reading frame on the complete DNA sequence of chromosome III. The putative Pel1 protein is characterized by a low molecular weight of approximately 17 kDa, a low codon adaptation index, and a high leucine content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00336781
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