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  • 1
    Electronic Resource
    Electronic Resource
    The Tup1-Ssn6 general repressor is involved in repression of IME1 encoding a transcriptional activator of meiosis in Saccharomyces cerevisiae (1998)
    Springer
    Current genetics 33 (1998), S. 239-247 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsSaccharomyces ; Tup1-Ssn6 repression ; IME1 ; Sin4-Rgr1 repression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ime1 plays a pivotal role in the initiation of meiosis in a/α diploid cells of Saccharomyces cerevisiae. In the absence of glucose and nitrogen, IME1 expression is greater in a/α cells than in either a or α cells and therefore only a/α, but not a/a or α/α, cells are committed to sporulation. It is known that IME1 expression is positively regulated by Mck1, Rim1, Ime4 and the Swi-Snf complex but other factors may also be involved. In addition, Rme1 is assumed to repress IME1 expression. To provide more details of the repression of expression of IME1, we have isolated mutants in which the IME1p-PHO5 fusion gene integrated at the ura3 locus is expressed in α cells under nutritionally rich conditions. We found that mutations occurred in TUP1, SSN6, SIN4 and RGR1, among which TUP1 and SSN6 were identified for the first time as negative regulators of IME1 expression. Deletion of the Rme1-binding site from the IME1 promoter did not result in activation of the expression of IME1 under nutritionally rich conditions, suggesting that Rme1 does not function as a DNA-binding protein with the Tup1-Ssn6 repression complex. We also demonstrated that the 294-bp fragment from nucleotide position –914 to –621 and the 301-bp fragment from nucleotide position –1215 to –915 of the IME1 promoter region contain elements acting as URS and UAS in TUP1 + and tup1 mutant cells, respectively. These findings indicate that IME1 is negatively regulated by the Tup1-Ssn6 repressor complex through two distinct upstream regions in conjunction with unidentified DNA-binding proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050332
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of Non-ADP-ribosylatable, Diphtheria Toxin-Resistant Elongation Factor 2 in Saccharomyces cerevisiae
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 191 (1993), S. 1145-1151 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/bbrc.1993.1336
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  • 3
    Electronic Resource
    Electronic Resource
    Assignment of (6R*,10R*)-relative stereochemistry to the major component of the sex pheromone of the maritime pine scale, matsucoccus feytaudi
    Amsterdam : Elsevier
    Tetrahedron Letters 32 (1991), S. 5995-5998 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(00)79447-0
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  • 4
    Electronic Resource
    Electronic Resource
    Sodium bis(2-methoxyethoxy)(1,1,1,3,3,3-hexafluoro-2-propoxy)aluminum hydride, a new stereoselective reducing agent in a carbacyclin synthesis
    Amsterdam : Elsevier
    Tetrahedron 47 (1991), S. 2773-2784 
    Details
    ISSN: 0040-4020
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)87084-8
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  • 5
    Electronic Resource
    Electronic Resource
    Assignment of(6R^p^*,10R^p^*)-realtive stereochemistryto to the major component of the sex pheromone of the maritime pine scale,Matsucoccus feytaudi
    Amsterdam : Elsevier
    Tetrahedron Letters 33 (1992), S. 282 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(00)74112-8
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  • 6
    Electronic Resource
    Electronic Resource
    Occurrence of genetic segregation in a putative haploid strain of Endomyces fibuliger met by spontaneous sectoring of protoplast fusants (1994)
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 465-471 
    Details
    ISSN: 1573-0972
    Keywords: Endomyces fibuliger ; genetic analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Detailed genetic analysis of Endomyces fibuliger, an amylolytic yeast which is homothallic and exists predominantly in the diploid state, has not been performed. From a naturally occurring strain, E. fibuliger 8014 met, a morphological mutant, 193 met, was obtained by u.v. mutagenesis. To obtain a haploid strain suitable for genetic analysis, an intergeneric hybrid between E. fibuliger 193 met and a strain of a closely related dimorphic heterothallic lipolytic yeast, Yarrowia lipolytica, A his1, was produced by mass mating. The intergeneric hybrid was highly unstable in vegetative culture on yeast extract/phosphate/soluble starch/agar media and produced numerous mitotic sectors. Most of the sectors were mitotically unstable. However, one mitotically stable sector, N14i60 met, was obtained which also differed from the strain 193 as gauged by the appearance of DNA bands on pulsed-field gel electrophoresis. The putative haploid strain, N14i60 met, had six bands whilst the mutant 193 met had seven. Ultra-violet treatment of cells of N14i60 met produced 19 auxotrophic mutants. Protoplast fusion between pairs of different mutants showed complementation and the fusants were unstable mitotically and gave unstable aneuploid and stable haploid sectors of parental and non-parental combinations of markers. It is postulated that complementary diploid fusants, which were obtained by protoplast fusion, produced sectors by mitotic non-disjunction. Such a mechanism provides a means to establish a genetic analysis system for E. fibuliger via the parasexual cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00144474
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  • 7
    Electronic Resource
    Electronic Resource
    The role of cysteine residues in the homeodomain protein Matα2 in mating-type control of Saccharomyces cerevisiae (1997)
    Springer
    Molecular genetics and genomics 255 (1997), S. 166-171 
    Details
    ISSN: 1617-4623
    Keywords: Key words Homeodomain protein ; Mating-type control ; Matα2 ; Disulfide bond ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Matα2 homeodomain protein plays a pivotal role in the control of cell type in Saccharomyces cerevisiae. The homeodomain in the C-terminal region of Matα2 functions as a DNA-binding domain and the N-terminal region, containing two cysteine residues at positions 33 and 34, is thought to be involved in formation of Matα2 homodimers via disulfide bonds. matα2 mutants, isolated in a previous study, in which haploid-specific genes cannot be repressed by the Mata1-Matα2 heterodimer but a-specific genes can be repressed by the Matα2 homodimer, were found to produce mutant Matα2 with a substitution of tyrosine or phenylalanine for Cys33. To clarify the role of Cys33 and Cys34 in the Matα2 protein, we generated several matα2 mutants by site-directed mutagenesis which had serine residues in place of these Cys residues. Transforming MAT a cells with plasmids carrying these matα2 (MATα1 +) mutations rendered transformants unable to mate. Northern blot analysis revealed that transcription of the a-specific gene STE2 and the haploid-specific locus RME1 in these transformants is repressed to the same level as in wild-type MAT a/MATα cells. We concluded that neither Cys33 nor Cys34 is required for repression of a-specific genes by the Matα2 homodimer or of haploid-specific genes by the Mata1-Matα2 heterodimer, and therefore suggest that Matα2 homodimer formation in vivo is not mediated by disulfide linkage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050485
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  • 8
    Electronic Resource
    Electronic Resource
    A putative membrane protein, Pho88p, involved in inorganic phosphate transport inSaccharomyces cerevisiae (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 580-590 
    Details
    ISSN: 1617-4623
    Keywords: Membrane proteins ; Phosphatase regulation ; Pho88p ; Pi transporter ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Transcription of a regulatory gene,PHO81, in the phosphatase regulon ofSaccharomyces cerevisiae is repressed by inorganic phosphate (Pi) in the medium via that same regulatory system. The activity of Pho81p, the product ofPHO81, is also inhibited by a high concentration of Pi in the medium. Increased dosage ofPHO86, a gene encoding a putative membrane protein associated with a Pi transporter complex, activates the Pi-inhibited Pho81p produced under the control of theGAL1 promoter. A new gene,PHO88/YBR106w, has now been identified as a multicopy suppressor of the rAPase− phenotype of the cells caused by theP i inhibition of Pho81p. Thepho86 disruptant expressed rAPase activity in high-Pi medium, while thepho88 disruptant did not. The Δpho86 Δpho88 double disruption resulted in enhanced synthesis of rAPase under the high-Pi condition and conferred arsenate resistance on the cells than those in single disruptants of these genes. Its hydropathy profile and the results of an analysis of its cellular localization suggested that Pho88p is a membrane protein similar to Pho86p. Both disruption and high dosage ofPHO88 orPHO86 resulted in reduced Pi uptake. These findings suggest that Pho88p is also involved in Pi transport and modulates Pho81p function together with Pho86p.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173648
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  • 9
    Electronic Resource
    Electronic Resource
    Activation of basal transcription by a mutation in SIN4, a yeast global repressor, occurs through a mechanism different from activator-mediated transcriptional enhancement (2000)
    Springer
    Molecular genetics and genomics 263 (2000), S. 48-59 
    Details
    ISSN: 1617-4623
    Keywords: Key words Basal transcription ; Sin4 repression ; Tup1-Ssn6 repression ; Rme1 repression ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae protein Sin4 has been suggested to affect the transcription of various genes by locally altering chromatin structure. Previous studies have defined two classes of promoters: those which are activated by loss of SIN4 function (termed sin4-responsive promoters) and those which are not activated by sin4 mutations (termed sin4 non-responsive promoters). We analyzed the mechanism of this differential response of the two classes of promoters to a sin4 mutation. The sin4 non-responsive promoters were activated when upstream elements in the promoter region were eliminated. The upstream elements of sin4 non-responsive promoters were, in turn, found to repress the activity of the sin4-responsive promoters in an orientation-independent manner. The sin4-mediated activation was repressed by the Rme1- but not by the Tup1-Ssn6-mediated repression system. Activation of sin4-responsive promoters by Pho4 and the sin4 mutation was additive, and enhancement of transcription driven by sin4-responsive promoters was found to be due to an increase in the basal rate of transcription. The upstream regions in the sin4 non-responsive promoters contained elements that were able to inhibit activation of basal transcription. Based on these observations, we suggest that activation of basal transcription by a mutation in a gene for a global repressor, SIN4, occurs through a mechanism that differs from that responsible for activator-mediated transcriptional enhancement, and we therefore propose that basal transcription and activator-mediated transcription are repressed by different mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008675
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning, sequencing, and functional analysis of H-OLE1 gene encoding Δ9-fatty acid desaturase in Hansenula polymorpha (2000)
    Springer
    Applied microbiology and biotechnology 54 (2000), S. 499-509 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract H-OLE1, a gene encoding Δ9-fatty acid desaturase (FAD) in Hansenula polymorpha strain CBS 1976, was isolated by hybridization based upon its homology with the P-OLE1 gene cloned earlier from a related species, Pichia angusta IFO 1475. The sequence of the H-OLE1 gene revealed high structural conservation with Δ9-FADs from various organisms. A putative 451-amino acid polypeptide encoded by the gene, like all other Δ9-FADs, contained two domains: an N-terminal catalytic domain containing three conserved histidine clusters, and a C-terminal cytochrome b 5-like domain which has been suggested to be involved in electron transport in desaturation reactions. The whole H-OLE1 gene complemented a H. polymorpha fad1 mutation leading to a defect in Δ9-FAD. However, the unsaturated fatty acid requirement that the Saccharomyces cerevisiae ole1 mutant displays was complemented by only the open reading frame of H-OLE1 driven by S. cerevisiae glyceroaldehyde-3-phosphate dehydrogenase promoter, but not by the intact H-OLE1, suggesting that the H. polymorphaΔ9-FAD was compatible with the desaturation system of S. cerevisiae whereas the promoter of the H-OLE1 gene had no activity in heterologous cells. It was shown by Northern hybridization that transcription of the H-OLE1 gene in H. polymorpha was slightly repressed by exogenous Δ9-unsaturated fatty acid. An H. polymorpha disruption mutant (ΔH-OLE1) was created by transformation of an fad1/FAD1 diploid with disrupted H-OLE1::S-LEU2 linear DNA. It was shown by genetic and molecular analyses that input DNA was integrated in several copies into the chromosomal target to replace the mutated fad1 allele. Gas chromatography analysis showed identical fatty acid compositions in cells of both fad1 and ΔHOLE1 disruption mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530000369
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