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  • 1
    Electronic Resource
    Electronic Resource
    Ethanol-induced and glucose-insensitive alcohol dehydrogenase activity in the yeast Kluyveromyces lactis (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The alcohol dehydrogenase (ADH) system in the yeast Kluyveromyces lactis is encoded by four ADH genes. In this paper we report evidence that at least three of these genes are transcribed and transcribed into protein. KIADH1 and KIADH2, which encode cytoplasmic activities, are preferentially expressed in glucose-grown cells with respect to ethanol-grown cells. KIADH4, which encodes one of the two activities localized within mitochondria, is induced at the transcriptional level in the presence of ethanol as is the ADH2 gene in Saccharomyces cerevlslae. However the regulation of the expression of the K. lactis gene is completely different from that of ADH2 and of other known ADH genes in that KIADH4 is insensitive to glucose repression and is not expressed on non-fermentabie carbon sources other than ethanol. This km6 of regulation can be clearly observed in non-fermenting strains, where the induction of KIADH4 is dependent on the addition of ethanol to the medium. On the contrary, in fermenting strains KIADH4 is always induced by ethanol or acetaldehyde produced endocellularly and this results in constitutive expression of the gene aiso in the presence of glucose. The mitochondrial localization of the activity encoded by KIADH4 and the peculiar regulation of this gene could be related to the fact that K. lactis is a petite negative yeast in which some mitochondrial functions seem to be essential for cell viability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb01403.x
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  • 2
    Electronic Resource
    Electronic Resource
    Suppression of a nuclear frameshift mutation by a mitochondrial tRNA in the yeast Kluyveromyces lactis (2002)
    Oxford, UK : Blackwell Science, Ltd
    Molecular microbiology 46 (2002), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A fragment of mitochondrial DNA containing the Kluyveromyces lactis gene for valine-tRNA (tRNAVAL) was isolated as a multicopy suppressor of a respiratory-deficient mutant of this yeast. The mutant produced a truncated Cox14p because of a +1 frameshift mutation in COX14, a nuclear gene encoding a protein imported into mitochondria which is necessary for respiration (Fiori et al. 2000 Yeast 16: 307–314). We report here that the mitochondrial tRNAVAL gene, when transformed into K. lactis cells, is transcribed outside mitochondria and suppresses the frameshift mutation in COX14 restoring the correct reading frame during translation of its mRNA. In fact, using histidine tagging, the existence of a suppressed Cox14p of normal length was demonstrated in mutants expressing the mt-tRNAVAL from the nucleus. Suppression could occur through a non-canonical four base pairing between the tRNAVAL and the mutated mRNA or through slippage of ribosomes during translation. This is a new case of informational suppression in that the suppression of a chromosomal mutation is not casused by a second mutation but to a mislocalization/expression of a mt-tRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2002.03147.x
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  • 3
    Electronic Resource
    Electronic Resource
    The mitochondrial DNA of the yeast Hansenula petersonii: genome organization and mosaic genes (1984)
    Springer
    Current genetics 8 (1984), S. 449-455 
    Details
    ISSN: 1432-0983
    Keywords: mtDNA ; Mosaic genes ; Genome organization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mitochondrial genomes of yeasts are circular DNA molecules that vary greatly in size in different species. The mitochondrial DNA of the yeast H. petersonii is about 42 kbp in length, about one half the size of the corresponding genome in S. cerevisiae. Sequences homologous to protein-encoding genes from S. cerevisiae have been identified and localized on this genome by hybridization with DNA from petite mutants. The comparison between the mitochondrial genomes of H. petersonii and S. cerevisiae showed differences in the overall genome organization, but both include genes with mosaic organization. In fact, sequences homologous to the first intron of the S. cerevisiae cob short gene are found in (or adjacent to) the cob and cox1 genes present in the genome of H. petersonii. Moreover, an intron homologous to that present in the 21S rRNA gene of S. cerevisiae seems to have been conserved in the large ribosomal RNA gene of H. petersonii, in a similar position.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00433911
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  • 4
    Electronic Resource
    Electronic Resource
    Transformation of the yeast Kluyveromyces lactis by new vectors derived from the 1.6 μm circular plasmid pKD1 (1987)
    Springer
    Current genetics 12 (1987), S. 185-192 
    Details
    ISSN: 1432-0983
    Keywords: Yeast plasmid ; Transformation ; pKD1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The circular plasmid pKD1 (or 1.6 μm DNA) has recently been isolated from Kluyveromyces drosophilarum. This plasmid appears to have a functional organization analogous to that of the 2 μ DNA of Saccharomyces cerevisiae, although the respective nucleotide sequences show little homology. pKD1 can be transferred to Kluyveromyces lactis where it is replicated stably. Using recombinant molecules derived from pKDl, a practical transformation system has been developed for Kluyveromyces lactis, with an efficiency and stability comparable to the 2 μ-based Saccharomyces cerevisiae transformation system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00436877
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  • 5
    Electronic Resource
    Electronic Resource
    Two mitochondrial alcohol dehydrogenase activities of Kluyveromyces lactis are differently expressed during respiration and fermentation (1995)
    Springer
    Molecular genetics and genomics 249 (1995), S. 665-672 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Kluyveromyces lactis ; Alcohol dehydrogenase ; Glucose and ethanol metabolism ; Transcriptional regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The lactose-utilizing yeast Kluyveromyces lactis is an essentially aerobic organism in which both respiration and fermentation can coexist depending on the sugar concentration. Despite a low fermentative capacity as compared to Saccharomyces cerevisiae, four structural genes encoding alcohol dehydrogenase (ADH) activities are present in this yeast. Two of these activities, namely KlADH III and KlADH IV, are located within mitochondria and their presence is dependent on the carbon sources in the medium. In this paper we demonstrate by transcription and activity analysis that KlADH3 is expressed in the presence of low glucose concentrations and in the presence of respiratory carbon sources other than ethanol. Indeed ethanol acts as a strong repressor of this gene. On the other hand, KlADH4 is induced by the presence of ethanol and not by other respiratory carbon sources. We also demonstrate that the presence of KlADH III and KlADH IV in K. lactis cells is dependent on glucose concentration, glucose uptake and the amount of ethanol produced. As a consequence, these activities can be used as markers for the onset of respiratory and fermentative metabolism in this yeast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418036
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  • 6
    Electronic Resource
    Electronic Resource
    Dependence of cytoplasmic on mitochondrial protein synthesis inK. lactis CBS 2360 (1977)
    Springer
    Molecular genetics and genomics 150 (1977), S. 137-140 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the “petite negative” yeastKluyveromyces lactis (strain CBS 2360) growth is inhibited by the same Erythromycin concentrations on fermentable and non-fermentable carbon sources. The minimal inhibitory concentration of Erythromycin does not affect respiration, but completely inhibits total aminoacid incorporation by the cells in conditions in which permeability effects can be ruled out. The effect of the antibiotic on the “in vitro” protein synthesis by cytoplasmic and mitochondrial systems shows that inhibition is effective only at the mitochondrial level. Results suggest that the inhibition of growth and of total protein synthesis is a consequence of the inhibition of mitochondrial protein synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00695393
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  • 7
    Electronic Resource
    Electronic Resource
    The alcohol dehydrogenase system in the yeast, Kluyveromyces lactis (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 6 (1990), S. 193-204 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces lactis ; alcohol dehydrogenase ; gene regulation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have studied the alcohol dehydrogenase (ADH) system in the yeast Kluyvefromyces lactis. Southern hybridization to the Saccharomyces cerevisiae ADH2 gene indicates four probable structural ADH genes in K. lactis. Two of these genes have been isolated from a genomic bank by hybridization to ADH2. The nucleotide sequence of one of these genes shows 80% and 50% sequence identity to the ADH genes of S. cerevisiae and Schizosaccharomyces pombe respectively. One K. lactis ADH gene is preferentially expressed in glucose-grown cells and, in analogy to S. cerevisiae, was named K1ADH1. The other gene, homologous to K1ADH1 in sequence, shows an amino-terminal extension which displays all of the characteristics of a mitochondrial targeting presequence. We named this gene K1ADH3. The two genes have been localized on different chromosomes by Southern hybridization to an orthogonal-field-alternation gel electrophoresis-resolved K. lactis genome. ADH activities resolved by gel electrophoresis revealed several ADH isozymes which are differently expressed in K. lactis cells depending on the carbon source.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320060304
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  • 8
    Electronic Resource
    Electronic Resource
    Two genes encoding putative mitochondrial alcohol dehydrogenases are present in the yeast Kluyveromyces lactis (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 391-400 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces lactis ; alcohol dehydrogenase ; mitochondrial import ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Four structural genes encoding isozymes of the alcohol dehydrogenase (ADH) system in the yeast Kluyveromyces lactis have been identified by hybridization to ADH2 DNA probes from Saccharomyces cerevisiae. In this paper we report on the isolation of KlADH4 and the complete sequencing of KlADH3 and KlADH4, two genes which show high homology to KlADH1, the ADH gene previously isolated in K. lactis, and to the ADH genes of S. cerevisiae. When compared with KlADH1, both KlADH3 and KlADH4 encode amino-terminal extensions which show the characteristics of the mitochondrial targeting sequences. These extensions are poorly conserved both at the nucleotide and the amino acid level. Suprisingly, the KlADH4 extension shows a higher identity at the amino acid level to the one encoded by ADH3 of S. cerevisiae than to the KlADH3 presequence. KlADH3 and KlADH4, in contrast to the ADH3 gene of S. cerevisiae, show a strong bias in the choice of codons.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320070409
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  • 9
    Electronic Resource
    Electronic Resource
    Glucose metabolism and ethanol production in adh multiple and null mutants of Kluyveromyces lactis (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1133-1140 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces lactis ; alcohol dehydrogenase ; ADH genes ; isozymes ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Four genes coding for alcohol dehydrogenase (ADH) activities were identified in Kluyveromyces lactis. Due to the presence in this yeast of multiple ADH isozymes, mutants in the individual genes constructed by gene replacement yielded no clear phenotype. We crossed these mutants and developed a screening procedure which allowed us to identify strains lacking several ADH activities. The analysis of the adh triple mutants revealed that each activity confers to the cell the ability to grow on ethanol as the sole carbon source. On the contrary, adh null strains failed to grow on this substrate, indicating that no other important ADH activities are present in K. lactis cells. In the adh null mutants we also found a residual production of ethanol, as has been reported to be the case in Saccharomyces cerevisiae. This production showed a ten-fold increase when the K1ADHI activity was reintroduced in the null mutant and cells were cultivated under oxygen-limiting conditions. Differently from S. cerevisiae, glycerol is poorly accumulated in K. lactis adh null mutants.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100902
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