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  • Articles  (12)
  • Yeast
  • Springer  (12)
  • Cambridge University Press
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  • Articles  (12)
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  • Springer  (12)
  • Cambridge University Press
  • Nature Publishing Group
  • Periodicals Archive Online (PAO)
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  • 1
    Electronic Resource
    Electronic Resource
    Xylanase from the psychrophilic yeast Cryptococcus adeliae (2000)
    Springer
    Extremophiles 4 (2000), S. 137-144 
    Details
    ISSN: 1433-4909
    Keywords: Key words Xylanases ; Psychrophile ; Yeast ; Molecular adaptation ; Molecular modeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A xylanase belonging to family 10 is produced by Cryptococcus adeliae, an Antarctic yeast that exhibits optimal growth at low temperature. The mature glycosylated xylanase secreted by C. adeliae is composed of 338 amino acid residues and 26 ± 3 osidic residues, and shares 84% identity with its mesophilic counterpart from C. albidus. The xylanase from C. adeliae is less thermostable than its mesophilic homologue when the residual activities are compared, and this difference was confirmed by differential scanning calorimetry experiments. In the range 0°–20°C, the cold-adapted xylanase displays a lower activation energy and a higher catalytic efficiency. All these observations suggest a less compact, more flexible molecular structure. Analysis of computerized molecular models built up for both psychrophilic and mesophilic xylanases indicates that the adaptation to cold consists of discrete changes in the tridimensional structure: of 53 substitutions, 22 are presumably involved in the adaptation process. These changes lead mainly to a less compact hydrophobic packing, to the loss of one salt bridge, and to a destabilization of the macrodipoles of the helices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920070028
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  • 2
    Electronic Resource
    Electronic Resource
    Mss51p, a putative translational activator of cytochrome c oxidase subunit-1 (COX1) mRNA, is required for synthesis of Cox1p in Saccharomyces cerevisiae (2000)
    Springer
    Current genetics 37 (2000), S. 213-220 
    Details
    ISSN: 1432-0983
    Keywords: Key words MSS51 ; Mitochondrial translation ; Yeast ; Cytochrome c oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Mutants of Saccharomyces cerevisiae that lack a functional MSS51 gene are respiratory deficient due to the absence of cytochrome c oxidase subunit 1 (Cox1p). It has been previously suggested, but not formally proven, that Mss51p is required for translational activation of COX1 mRNA, rather than being involved in a subsequent step in the synthesis of Cox1p or its assembly into cytochrome c oxidase. Pulse-chase labelling experiments now show that the absence of detectable levels of Cox1p in mss51-null strains is indeed due to the lack of synthesis of Cox1p, and is not caused by reduced stability of the protein. To gain more insight into the exact function of Mss51p, we determined the subcellular localization of the protein. We were able to show that an epitope-tagged version of Mss51p (Mss51HA) complements the mutation and can be localized in mitochondria, where it is firmly associated with the mitochondrial inner membrane. In addition, we characterized the previously identified mutant allele mss51-3. Sequence analysis revealed the presence of a short open reading frame upstream of MSS51 resulting from the creation of an extra ATG startcodon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050522
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and RNA-binding analysis of NAD+-isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe (2000)
    Springer
    Current genetics 38 (2000), S. 87-94 
    Details
    ISSN: 1432-0983
    Keywords: Key words Mitochondrial translation ; RNA binding ; Isocitrate dehydrogenase ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Krebs cycle NAD+-isocitrate dehydrogenase (Idh) binds to the 5-UTRs of all mitochondrial mRNAs in Saccharomyces cerevisiae. We hypothesize that this leader-binding activity plays a role in translational regulation, thereby linking mitochondrial biogenesis to the need for respiratory function. Analysis of effects of leader binding on mitochondrial translation is complicated by the involvement of the enzyme in mitochondrial metabolism. We have therefore searched for an Idh altered in RNA binding, but retaining full enzyme activity. Idh from Kluyveromyces lactis and Schizosaccharomyces pombe was partially purified and examined for the ability to bind Cox2 mRNA. Sch. pombe Idh, like the S. cerevisiae enzyme, has high affinity for both its own, K. lactis and S. cerevisiaeCOX2 leaders. In contrast, Idh purified from K. lactis shows only low affinity for all mRNAs tested. To determine what distinguishes K. lactis Idh from S. cerevisiae Idh, genes encoding the two subunits of Idh in K. lactis were cloned and sequenced. Sequence comparison revealed high levels of similarity throughout the proteins, in particular in regions involved in enzyme activity, co-factor and regulator binding. Non-conserved residues between the subunits from the two yeasts are candidates for involvement in the interaction with RNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940000132
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  • 4
    Electronic Resource
    Electronic Resource
    Influence of homology size and polymorphism on plasmid integration in the yeast CYC1 DNA region (2000)
    Springer
    Current genetics 37 (2000), S. 292-297 
    Details
    ISSN: 1432-0983
    Keywords: Key words DNA homology ; Recombination ; Integrative plasmids ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We studied the influence of homology size and polymorphism on the integration of circular plasmids into the yeast CYC1 region. The plasmids used also contained the URA3 gene, and the proportion of Ura+ transformants resulting from plasmid integration into the CYC1 region was determined by Southern-blot analysis. A size-dependent decrease in integration into the CYC1 region was observed from 858 bp to 363 bp of homology. However, with a homology size of 321, 259 or 107 bp, about 2% of the transformants still contained plasmid molecules integrated in the CYC1 region. A single point mutation in the 858-bp fragment decreased the proportion of integrations to the CYC1 gene, but the presence of additional mutations did not have a cumulative effect. For plasmids isolated in a single-stranded (ss) form, the presence of two or six point mutations did not influence integration. These results were compared with those obtained in other assays designed to study substrate requirements for homologous recombination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050530
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  • 5
    Electronic Resource
    Electronic Resource
    Characterisation of a tripartite nuclear localisation sequence in the regulatory protein Lys14 of Saccharomyces cerevisiae (2000)
    Springer
    Current genetics 38 (2000), S. 78-86 
    Details
    ISSN: 1432-0983
    Keywords: Key words Nuclear import ; Lys14p ; Lysine ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The Lys14 regulatory protein of Saccharomyces cerevisiae activates the expression of the LYS genes involved in the lysine biosynthetic pathway. Studies with a fused Lys14-green fluorescent protein reveal that Lys14p is localised to the nucleus, even under growth conditions leading to the absence of LYS gene expression. Lys14p nuclear localisation is mediated by a tripartite sequence made up of three short basic motifs located on the C-terminal side of the Zn cluster domain of Lys14p. Substitution of basic residues by alanines in any of the three motifs partially prevents the nuclear import of the protein. Simultaneous mutations in the three basic domains are required to completely abolish the entry into the nucleus and to impair the Lys14 function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940000134
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of novel rad6/ubc2 ubiquitin-conjugating enzyme mutants in yeast (2000)
    Springer
    Current genetics 37 (2000), S. 221-233 
    Details
    ISSN: 1432-0983
    Keywords: Key Words Rad6 ; Ubiquitination ; Silencing ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Null mutations in the RAD6/UBC2 gene encoding an E2 ubiquitin-conjugating enzyme cause deficiencies in DNA repair, N-end-rule protein degradation, sporulation and telomeric silencing, and alter the preferred integration positions for Ty1 retrotransposons. Here we selected for mutants of RAD6 that cause a release of telomeric silencing. Some alleles retained nearly wild-type ability for sporulation, DNA repair and the degradation of proteins. Alteration in Ty1 integration-site bias accompanied some of these alleles. The possibility that some mutations specifically affect binding of an unknown protein that works with Rad6 in its silencing role, but is not required for DNA repair or N-end-rule activity, is discussed in terms of the Rad6 crystal structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050523
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  • 7
    Electronic Resource
    Electronic Resource
    The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis (2000)
    Springer
    JBIC 5 (2000), S. 189-203 
    Details
    ISSN: 1432-1327
    Keywords: Key words Copper ; Zinc ; Superoxide dismutase ; Amyotrophic lateral sclerosis ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have investigated factors that influence the properties of the zinc binding site in yeast copper-zinc superoxide dismutase (CuZnSOD). The properties of yeast CuZnSOD are essentially invariant from pH 5 to pH 9. However, below this pH range there is a change in the nature of the zinc binding site which can be interpreted as either (1) a change in metal binding affinity from strong to weak, (2) the expulsion of the metal bound at this site, or (3) a transition from a normal distorted tetrahedral ligand orientation to a more symmetric arrangement of ligands. This change is strongly reminiscent of a similar pH-induced transition seen for the bovine protein and, based on the data presented herein, is proposed to be a property that is conserved among CuZnSODs. The transition demonstrated for the yeast protein is not only sensitive to the pH of the buffering solution but also to the occupancy and redox status of the adjacent copper binding site. Furthermore, we have investigated the effect of single site mutations on the pH- and redox-sensitivity of Co2+ binding at the zinc site. Each of the mutants H46R, H48Q, H63A, H63E, H80C, G85R, and D83H is capable of binding Co2+ to a zinc site with a distorted tetrahedral geometry similar to that of wild-type. However, they do so only if Cu+ is bound at the copper site or if the pH in raised to near physiological levels, indicating that the change at the zinc binding site seen in the wild-type is conserved in the mutants, albeit with an altered pK a. The mutants H71C and D83A did not bind Co2+ in a wild-type-like fashion under any of the conditions tested. This study reveals that the zinc binding site is exquisitely sensitive to changes in the protein environment. Since three of the mutant yeast proteins investigated here contain mutations analogous to those that cause ALS (amyotrophic lateral sclerosis) in humans, this finding implicates improper metal binding as a mechanism by which CuZnSOD mutants exert their toxic gain of function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050363
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  • 8
    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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  • 9
    Electronic Resource
    Electronic Resource
    Protein phosphatase type-1 regulatory subunits Reg1p and Reg2p act as signal transducers in the glucose-induced inactivation of maltose permease in Saccharomyces cerevisiae (2000)
    Springer
    Molecular genetics and genomics 263 (2000), S. 411-422 
    Details
    ISSN: 1617-4623
    Keywords: Key words Maltose permease ; REG1 ; 2 ; Glucose signaling ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The REG1 gene encodes a regulatory subunit of the type-1 protein phosphatase (PP1) Glc7 in Saccharomyces cerevisiae, which directs the catalytic subunit to substrates involved in glucose repression. Loss of REG1 relieves glucose repression of many genes, including the MAL structural genes that encode the maltose fermentation enzymes. In this report, we explore the role of Reg1p and its homolog Reg2p in glucose-induced inactivation of maltose permease. Glucose stimulates the proteolysis of maltose permease and very rapid loss of maltose transport activity – more rapid than can be explained by loss of the permease protein alone. In a reg1Δ strain we observe a significantly reduced rate of glucose-induced proteolysis of maltose permease, and the rapid loss of maltose transport activity does not occur. Instead, surprisingly, the slow rate of proteolysis of maltose permease is accompanied by an increase in maltose transport activity. Loss of Reg2p modestly reduces the rates of both glucose-induced proteolysis of maltose permease and inactivation of maltose transport activity. Overexpression of Reg2p in a reg1Δ strain suppresses the effect on maltose permease proteolysis and partially restores the inactivation of maltose transport activity, but does not affect the insensitivity of MAL gene expression to repression by glucose observed in this strain. Thus, protein phosphatase type-1 (Glc7p-Reg1p and Glc7p-Reg2p) plays a role in transduction of the glucose signal during glucose-induced proteolysis of maltose permease, but only Glc7p-Reg1p is involved in glucose-induced inactivation of maltose transport activity and glucose repression of MAL gene expression. Overexpression of REG1 partially restores proteolysis of maltose permease in a grr1Δ strain, which lacks glucose signaling, but does not rescue rapid inactivation of maltose transport activity or sensitivity to glucose repression. A model for the role of Reg1p and Reg2p in glucose signaling pathways is discussed. We also uncovered a previously unrecognized G2/M delay in the grr1Δ but not the reg1Δ strains, and this delay is suppressed by REG1 overexpression. The G1/S delay seen in grr1Δ mutants is slightly suppressed as well, but REG1 overexpression does not suppress other grr1Δ phenotypes such as insensitivity to glucose repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051185
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  • 10
    Electronic Resource
    Electronic Resource
    Telomeric silencing of a natural subtelomeric gene (2000)
    Springer
    Molecular genetics and genomics 263 (2000), S. 287-291 
    Details
    ISSN: 1617-4623
    Keywords: Keywords Silencing ; Telomeres ; Heterochromatin ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The heterochromatin at telomeres can repress the expression of reporter genes when they are transplanted into their vicinity. Although this transcriptional silencing has been widely characterized using reporter genes, the ability of telomeres to repress natural subtelomeric genes has remained uncertain. In a previous report we described telomeric silencing of a yeast retrotransposon. Here we describe the identification of a subtelomeric gene from Saccharomyces cerevisiae that is subject to natural telomeric silencing. In addition, we show that telomeric silencing is not a general feature of the first ORFs located adjacent to Telomere-Associated Sequences.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051170
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