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  • 550 - Earth sciences
  • Chemical Engineering
  • General Chemistry
  • Humans
  • Saccharomyces cerevisiae
  • Springer  (55)
  • 2000-2004  (20)
  • 1975-1979  (35)
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  • 1
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    Early warning systems for natural disaster reduction (2003)
    Springer
    Details
    Publication Date: 2020-02-12
    Keywords: 550 - Earth sciences
    Type: info:eu-repo/semantics/book
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  • 2
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    GPS : theory, algorithms and applications (2003)
    Springer
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    Publication Date: 2020-02-12
    Keywords: 550 - Earth sciences
    Type: info:eu-repo/semantics/book
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  • 3
    Electronic Resource
    Electronic Resource
    A gene of the major facilitator superfamily encodes a transporter for enterobactin (Enb1p) in Saccharomyces cerevisiae (2000)
    Springer
    BioMetals 13 (2000), S. 65-72 
    Details
    ISSN: 1572-8773
    Keywords: major facilitator superfamily ; iron transport ; siderophores ; enterobactin ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract While in fungi iron transport via hydroxamate siderophores has been amply proven, iron transport via enterobactin is largely unknown. Enterobactin is a catecholate-type siderophore produced by several enterobacterial genera grown in severe iron deprivation. By using the KanMX disruption module in vector pUG6 in a fet3Δ background of Saccharomyces cerevisiae we were able to disrupt the gene YOL158c Sce of the major facilitator super family (MFS) which has been previously described as a gene encoding a membrane transporter of unknown function. Contrary to the parental strain, the disruptant was unable to utilize ferric enterobactin in growth promotion tests and in transport assays using 55Fe-enterobactin. All other siderophore transport properties remained unaffected. The results are evidence that in S. cerevisiae the YOL158c Sce gene of the major facilitator super family, now designated ENB1, encodes a transporter protein (Enb1p), which specifically recognizes and transports enterobactin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009250017785
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  • 4
    Electronic Resource
    Electronic Resource
    Altered patterns of protein synthesis induced by heat shock of yeast (1979)
    Springer
    Current genetics 1 (1979), S. 63-74 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Translation ; Coordinate regulation ; Electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The products of protein synthesis from exponential phase cultures of Saccharomyces cerevisiae grown at 23 °C or at 36 °C appear to be essentially identical. However, yeast cells respond to a shift in culture temperature from 23 °C to 36 °C with the rapid de novo synthesis of a polypeptide species of molecular weight 100,000. Within 60–90 min after the shift this polypeptide represents approximately 2.5% of the total cellular protein, a 5–10 fold increase over the preshift level. The level of this polypeptide then decreases with continued growth of the cells at 36 °C. Analyses by SDS-polyacrylamide gel electrophoresis of polypeptides obtained from cells pulse labeled with [35S]methionine demonstrate that following a temperature shift from 23 °C to 36 °C the synthetic rate of the 100,000 molecular weight polypeptide (as well as a number of other polypeptide species) increases to a level at least 10 fold higher than that observed prior to the shift. A concomittant decrease is observed in the synthesis of a large number of polypeptide species which were actively synthesized before the shift. Maximum changes in synthetic rates are observed 20–30 min after the shift and preshift synthetic patterns are regained within 60–90 min. Synthetic changes of the same magnitude and time course can be produced by short (20–30 min) exposures to 36 °C implicating a heat shock response. Several of the transiently induced polypeptides, including the 100,000 molecular weight species, show an affinity for DNA as determined by DNA-cellulose chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413307
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  • 5
    Electronic Resource
    Electronic Resource
    A screen of yeast respiratory mutants for sensitivity against the mycotoxin citrinin identifies the vacuolar ATPase as an essential factor for the toxicity mechanism (2000)
    Springer
    Current genetics 37 (2000), S. 227-284 
    Details
    ISSN: 1432-0983
    Keywords: Key words Citrinin ; Pet mutants ; Mitochondrial biogenesis ; Vacuolar ATPase ; YKL118W disruption ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In countries with a hot climate the mycotoxin citrinin represents a serious problem in fungal food-poisoning. In humans the renal system is affected the most and the mitochondrial respiratory chain was identified as a possible sensitive target for this toxin. In addition, citrinin has an antifungal activity that also inhibits the growth of the yeast Saccharomyces cerevisiae. So far the precise mode of action and the subcellular targets for citrinin have not been identified. Therefore, we decided to use the model organism yeast for a genetic approach to identify genes that play a role in the sensitivity against this mycotoxin. A large collection of conditional respiratory deficient yeast mutants was screened for sensitivity against citrinin. One special pet-ts mutant was identified that exhibited a higher sensitivity against citrinin. The genetic system of yeast allowed the isolation of the respective wild-type gene. This yeast gene encodes the Vph2p subunit that is essential for the correct assembly of the vacuolar ATPase. Isolation of the mutated gene and gene-disruption experiments of VPH2 and the partially overlapping small YKL118W gene verified this finding. The wild-type VPH2 gene restores all defects of the mutants. In contrast to this, YKL118W gave no complementation and the null mutant showed no phenotype. Thereby the yeast vacuolar ATPase was found to be important for the toxic effect of citrinin in yeast cells. The consequences of this finding for the molecular mechanism of citrinin action and its relation to the mitochondrial respiratory chain are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940070001
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  • 6
    Electronic Resource
    Electronic Resource
    POL32, a subunit of the Saccharomyces cerevisiae DNA polymerase δ, defines a link between DNA replication and the mutagenic bypass repair pathway (2000)
    Springer
    Current genetics 38 (2000), S. 178-187 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsPOL32 ; SRS2 ; DNA repair ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pol32 is a subunit of Saccharomyces cerevisiae DNA polymerase δ required in DNA replication and repair. To gain insight into the function of Pol32 and to determine in which repair pathway POL32 may be involved, we extended the analysis of the pol32Δ mutant with respect to UV and methylation sensitivity, UV-induced mutagenesis; and we performed an epistasis analysis of UV sensitivity by combining the pol32Δ with mutations in several genes for postreplication repair (RAD6 group), nucleotide excision repair (RAD3 group) and recombinational repair (RAD52 group). These studies showed that pol32Δ is deficient in UV-induced mutagenesis and place POL32 in the error-prone RAD6/REV3 pathway. We also found that the increase in the CAN1 spontaneous forward mutation of different rad mutators relies entirely or partially on a functional POL32 gene. Moreover, in a two-hybrid screen, we observed that Pol32 interacts with Srs2, a DNA helicase required for DNA replication and mutagenesis. Simultaneous deletion of POL32 and SRS2 dramatically decreases cellular viability at 15 °C and greatly increases cellular sensitivity to hydroxyurea at the permissive temperature. Based on these findings, we propose that POL32 defines a link between the DNA polymerase and helicase activities, and plays a role in the mutagenic bypass repair pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940000149
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  • 7
    Electronic Resource
    Electronic Resource
    Endopolygalacturonase genes and enzymes from Saccharomyces cerevisiae and Kluyveromyces marxianus (2000)
    Springer
    Current genetics 38 (2000), S. 264-270 
    Details
    ISSN: 1432-0983
    Keywords: Key words Endopolygalacturonase ; Saccharomyces cerevisiae ; Kluyveromyces marxianus ; Pectinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene encoding endopolygalacturonase (EC 3.2.1.15) has been cloned, sequenced and expressed from three strains of Saccharomyces cerevisiae (including non-secretors) and three strains of Kluyveromyces marxianus. Both control and coding regions showed small differences within each species, one including loss of a potential glycosylation site. Two non-secreting S. cerevisiae strains (FY1679 and var. uvarum) had non-transcribed copies of functional genes. Maximum enzyme activity was achieved with the S. cerevisiae FY1679 gene in an expressing vector, with an enzyme activity of 51 μmol of reducing sugar released from polygalacturonic acid μg protein−1 min−1, the highest so far reported for a yeast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940000160
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  • 8
    Electronic Resource
    Electronic Resource
    Recessive mutations in SUP35 and SUP45 genes coding for translation release factors affect chromosome stability in Saccharomyces cerevisiae (2000)
    Springer
    Current genetics 37 (2000), S. 285-291 
    Details
    ISSN: 1432-0983
    Keywords: Key words Translation release factors ; Chromosome stability ; Microtubules ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromosome stability in suppressor mutants for SUP35 and SUP45 genes coding for translation release factors was studied. We obtained spontaneous and UV-induced sup35 or sup45 mutants in a haploid strain disomic for chromosome III and tested the stability of an extra copy of this chromosome. The majority of the mutants showed increased chromosome instability. This phenotype was correlated with an increased sensitivity to the microtubule-poisoning drug benomyl which affects chromosome segregation at anaphase. Our data suggest that termination-translation factors eRF3 and eRF1 control chromosome transmission at mitotic anaphase in Saccharomyces cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050529
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  • 9
    Electronic Resource
    Electronic Resource
    Free tryptophan pool and tryptophan biosynthetic enzymes in Saccharomyces cerevisiae (1976)
    Springer
    Archives of microbiology 107 (1976), S. 207-214 
    Details
    ISSN: 1432-072X
    Keywords: Anthranilate synthase ; Cell permeabilisation ; Indoleglycerolphosphate synthase ; Saccharomyces cerevisiae ; Tryptophan biosynthetic enzymes ; Tryptophan pool
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The free tryptophan pool and the levels of two enzymes of tryptophan biosynthesis (anthranilate synthase and indoleglycerolphosphate synthase) have been determined in a wild type strain of Saccharomyces cerevisiae and in mutants with altered regulatory properties. The tryptophan pool of wild type cells growing in minimal medium is 0.07 μmole per g dry weight. Addition of anthranilate, indole or tryptophan to the medium produces a fifteen- to forty-fold increase in tryptophan pool, but causes no repression of the biosynthetic enzymes. Inclusion of 5-methyltryptophan in the growth medium causes a reduction in growth rate and a derepression of the biosynthetic enzymes, and this is shown here not to be correlated with a decrease in the free tryptophan pool. Mutants with an altered anthranilate synthase showing decreased sensitivity to inhibition by l-tryptophan or by the analogue dl-5-methyltryptophan have a tryptophan pool far higher than the wild type strain, but no repression of indoleglycerolphosphate synthase was observed. Mutants with an anthranilate synthase more sensitive to tryptophan inhibition show a slightly reduced tryptophan pool, but no derepression of indoleglycerolphosphate synthase was found. A mutant with constitutively derepressed levels of the biosynthetic enzymes shows a considerably increased tryptophan pool. Addition of 5-methyltryptophan to the growth medium of non-derepressible mutants causes a decrease in growth rate accompanied by a decrease in the tryptophan pool.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446842
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  • 10
    Electronic Resource
    Electronic Resource
    Some physiological observations on the uptake of d-glucose and 2-deoxy-d-glucose by starving and exponentially-growing yeasts (1976)
    Springer
    Archives of microbiology 111 (1976), S. 185-192 
    Details
    ISSN: 1432-072X
    Keywords: Yeasts ; Sugars ; d-Glucose ; 2-Deoxy-d-glucose ; Pichia pinus ; Transport ; Starvation ; Exponential growth ; Methodology ; Candida utilis ; Saccharomyces cerevisiae ; Rhodosporidium toruloides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Some methods for measuring the uptake of sugars by yeasts were investigated critically. A study was made of the effects of starvation of Pichia pinus, Candida utilis, Saccharomyces cerevisiae and Rhodosporidium toruloides on their uptake of d-glucose and 2-deoxy-d-glucose. Marked changes in the rates of uptake of these sugars occurred during 10 h of starvation, including (a) an immediate increase of up to 75% above that for growing cells and (b) a continuous decline to as little as 4%. Each yeast behaved differently. The rates did not remain constant during the periods of starvation often used for studies on the transport of sugars into yeasts. For Pichia pinus, there were striking differences, associated with starvation, between the transport of 2-deoxy-d-glucose and d-glucose, despite evidence that the two sugars enter this yeast by means of the same carrier. Some physiological explanations for these findings are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446567
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