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  • 1
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    Activation of Gal4p by galactose-dependent interaction of galactokinase and Gal80p (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Yeast galactokinase (Gal1p) is an enzyme and a regulator of transcription. In addition to phosphorylating galactose, Gal1p activates Gal4p, the activator of GAL genes, but the mechanism of this regulation has been unclear. Here, biochemical and genetic evidence is presented to show that Gal1p activates Gal4p by direct interaction with the Gal4p inhibitor Gal80p. Interaction requires galactose, adenosine triphosphate, and the regulatory function of Gal1p. These data indicate that Gal1p-Gal80p complex formation results in the inactivation of Gal80p, thereby transmitting the galactose signal to Gal4p.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zenke, F T -- Engles, R -- Vollenbroich, V -- Meyer, J -- Hollenberg, C P -- Breunig, K D -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1662-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Mikrobiologie, Heinrich-Heine-Universitat Dusseldorf, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Coenzymes/metabolism ; DNA-Binding Proteins ; Fungal Proteins/*metabolism ; Galactokinase/genetics/*metabolism ; Galactose/*metabolism ; Kluyveromyces/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Repressor Proteins/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
    Electronic Resource
    Electronic Resource
    Multicopy plasmids containing the gene for the transcriptional activator LAC9 are not tolerated by K. lactis cells (1989)
    Springer
    Current genetics 15 (1989), S. 143-148 
    Details
    ISSN: 1432-0983
    Keywords: 2-μm-like plasmid pKD1 ; Overexpression of transcription factors ; LAC9-GAL4 homology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The high copy number 2-μm DNA-like Kluyveromyces plasmid pKD1 was extremely unstable in Kluyveromyces lactis when carrying the gene for the regulatory protein LAC9, a transcriptional activator involved in the induction of the LAC and GAL genes. Transformants of a lac9 mutant strain normally contained rearranged plasmids and all were Lac−, indicating that the LAC9 gene was inactive. Lac+ “revertants” could be obtained from Lac− transformants by selection on lactose plates. In some of these, the pKD1-based plasmid was stably maintained by being integrated into the chromosome of the cell; in others, the disrupted chromosomal gene was restored by a gene conversion event. None of the Lac+ revertants had more than one intact LAC9 gene, an indication that LAC9 overexpression affects cell viability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00435461
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of the Arxula adeninivorans glucoamylase gene in Kluyveromyces lactis (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 102-106 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The glucoamylase gene of the yeast Arxula adeninivorans was expressed in Kluyveromyces lactis by using the GAP promoter from Saccharomyces cerevisiae and a multicopy plasmid vector. The transformants secreted 90.1% of the synthesized glucoamylase into the culture medium. The secreted glucoamylase activities are about 20 times higher in comparison to those of Saccharomyces cerevisiae transformants using the same promoter. Secreted glucoamylase possesses identical N-terminal amino acid sequences to those secreted by A. adeninivorans showing that cleavage of the N-terminal signal peptide takes place at the same site. Biochemical characteristics of glucoamylase expressed by K. lactis and A. adeninivorans are very similar.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050655
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  • 4
    Electronic Resource
    Electronic Resource
    Glucose repression of LAC gene expression in yeast is mediated by the transcriptional activator LAC9 (1989)
    Springer
    Molecular genetics and genomics 216 (1989), S. 422-427 
    Details
    ISSN: 1617-4623
    Keywords: Catabolite repression ; β-Galactosidase ; LAC9-GAL4 homology ; Kluyveromyces lactis ; Gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the yeast Kluyveromyces lactis the β-galactosidase gene is induced by lactose or galactose. As shown here it can also be repressed by glucose but only in some strains. When the LAC9 gene of a repressible strain is substituted by an allele of a non-repressible strain, the β-galactosidase gene is no longer glucose repressed. LAC9 codes for a regulatory protein homologous to GAL4 which activates transcription in the presence of the inducer. Since the LAC9 product is also present in the repressed strain and binds to DNA in vitro, as shown by DNA footprinting, glucose repression cannot be caused by repression of LAC9 gene expression. Instead, our results demonstrate that glucose repression is mediated by the LAC9 gene product, and is separable from the ability of LAC9 to activate transcription.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334386
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  • 5
    Electronic Resource
    Electronic Resource
    Differences in regulation of yeast gluconeogenesis revealed by Cat8p-independent activation of PCK1 and FBP1 genes in Kluyveromyces lactis (2000)
    Springer
    Molecular genetics and genomics 264 (2000), S. 193-203 
    Details
    ISSN: 1617-4623
    Keywords: Kluyveromyces lactis Carbon source regulation CAT8
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The yeast Kluyveromyces lactis can utilise a wide range of non-fermentable carbon compounds as sole sources of carbon and energy, and differs from Saccharomyces cerevisiae in being able to carry out oxidative and fermentative metabolism simultaneously. In S. cerevisiae, growth on all non-fermentable carbon sources requires Cat8p, a transcriptional activator that controls the expression of gluconeogenic and glyoxylate cycle genes via CSREs (Carbon Source Responsive Elements). The down-regulation of Cat8p by fermentable carbon sources is the primary factor responsible for the tight repression of gluconeogenesis by glucose in S. cerevisiae. To analyse the regulation of gluconeogenesis in K. lactis, we have cloned and characterised the K. lactis homologue of CAT8 (KlCAT8). The gene was isolated by multicopy suppression of a fog2/klsnf1 mutation, indicating a similar epistatic relationship between KlSNF1 and KlCAT8 as in the case of the S. cerevisiae homologues. KlCAT8 encodes a protein of 1445 amino acids that is 40% identical to ScCat8p. The most highly conserved block is the putative Zn(II)2Cys6 DNA-binding domain, but additional conserved regions shared with members of the zinc-cluster family from Aspergillus define a subfamily of Cat8p-related proteins. KlCAT8 complements the growth defect of a Sccat8 mutant on non-fermentable carbon sources. In K. lactis, deletion of KlCAT8 severely impairs growth on ethanol, acetate and lactate, but not on glycerol. Derepression of enzymes of the glyoxylate cycle – malate synthase and particularly isocitrate lyase – was impaired in a Klcat8 mutant, whereas Northern analysis revealed that derepression of KlFBP1 and KlPCK1 does not require KlCat8p. Taken together, our results indicate that in K. lactis gluconeogenesis is not co-regulated with the glyoxylate cycle, and only the latter is controlled by KlCat8p.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380000314
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  • 6
    Electronic Resource
    Electronic Resource
    Glucose repression of the Kluyveromyces lactis invertase gene KlINV1 does not require Mig1p (1999)
    Springer
    Molecular genetics and genomics 261 (1999), S. 862-870 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsKluyveromyces lactis ; Glucose repression ; INV1 ; MIG1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Kluyveromyces lactis, a budding yeast related to Saccharomyces cerevisiae, can grow on a wider variety of substrates and shows less sensitivity to glucose repression than does Saccharomyces cerevisiae. Many genes that are subject to glucose repression in S. cerevisiae are repressed only weakly or not at all in K. lactis. The molecular basis for this difference is largely unknown. To compare the mechanisms that regulate glucose repression in K. lactis and S. cerevisiae, we decided to clone and analyse an invertase gene from K. lactis. The SUC2 gene, which encodes invertase in S. cerevisiae, is strongly regulated by glucose and serves as a model system for studies on glucose repression. The invertase gene of K. lactis, KlINV1, was isolated by colony hybridization using a conserved region within the inulinase gene of K. marxianus as a probe. Two independent clones obtained were shown to contain the same ORF of 1827 bp. The deduced amino acid sequence is 59% similar to that of the K. marxianus inulinase and shows 49% similarity to ScSuc2p. Gene disruption experiments and low-stringency Southern analysis indicate that KlINV1 is a unique gene in K. lactis. Northern analysis revealed that the transcription of KlINV1 is strongly repressed in the presence of glucose, but, in contrast to the case in S. cerevisiae, repression is independent of KlMig1p.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050030
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  • 7
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    Molecular basis of tRNA recognition by the Elongator complex (2019)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of tRNA recognition and its modification reaction remain elusive. Here, we show cryo–electron microscopy structures of the catalytic subcomplex of Elongator and its tRNA-bound state at resolutions of 3.3 and 4.4 Å. The structures resolve details of the catalytic site, including the substrate tRNA, the iron-sulfur cluster, and a SAM molecule, which are all validated by mutational analyses in vitro and in vivo. tRNA binding induces conformational rearrangements, which precisely position the targeted anticodon base in the active site. Our results provide the molecular basis for substrate recognition of Elongator, essential to understand its cellular function and role in neurodegenerative diseases and cancer.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Expression of the Arxula adeninivorans glucoamylase gene in Kluyveromyces lactis (1996)
    Springer
    Details
    Publication Date: 1996-03-01
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
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  • 9
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    Multicopy plasmids containing the gene for the transcriptional activator LAC9 are not tolerated by K. lactis cells (1989)
    Springer
    Details
    Publication Date: 1989-02-01
    Print ISSN: 0172-8083
    Electronic ISSN: 1432-0983
    Topics: Biology
    Published by Springer
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  • 10
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    Activation of Gal4p by Galactose-Dependent Interaction of Galactokinase and Gal80p (1996)
    American Association for the Advancement of Science
    Details
    Publication Date: 1996-06-14
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science
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