ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
Your search history is empty.
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Analysis of a transketolase gene from Kluyveromyces lactis reveals that the yeast enzymes are more related to transketolases of prokaryotic origins than to those of higher eukaryotes (1997)
    Springer
    Current genetics 31 (1997), S. 15-21 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsKluyveromyces lactis ; Transketolase ; Evolution ; Carbohydrate metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The role of the pentose-phosphate pathway in carbohydrate metabolism of the yeast Kluyveromyces lactis, and the evolutionary relationships between the encoding genes, was investigated. For this purpose, we isolated the gene encoding transketolase (KlTKL1) and determined its nucleotide sequence. Surprisingly, comparisons of the deduced amino-acid sequence with those from other organisms revealed that the yeast enzymes are more related to those from prokaryotic sources than to those from higher eukaryotes. Functional analyses showed that KlTKL1 also complemented a Saccharomyces cerevisiae tkl1 tkl2 double mutant for growth in the absence of aromatic amino acids and restored transketolase activity in this mutant. A band detected in these transformants by Western-blot analysis corresponded to a band detected in K. lactis both in a wild-type strain and in a multicopy transformant with elevated transketolase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050171
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Transcriptional control of yeast phosphofructokinase gene expression
    Amsterdam : Elsevier
    FEBS Letters 289 (1991), S. 77-82 
    Details
    ISSN: 0014-5793
    Keywords: Glycolytic gene ; Promotor ; Saccharomyces cerevisiae
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(91)80912-M
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized through the pentose phosphate pathway (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have isolated the gene encoding transaldolase from Kluyveromyces lactis (KITALI) by screening a genomic library of this yeast using the TAL1 gene of Saccharomyces cerevisiae as a radioactive probe. The clone isolated contained an open reading frame of 1002 bp, encoding a protein with 76% identical residues in the deduced amino acid sequences as compared to Tal from S. cerevisiae. KITAL1 can complement a tal1 deletion of S. cerevisiae for enzymatic activity. The transcription start of KITAL1 was located at -69 bp relative to the ATG translation start codon. Deleting a large part of the open reading frame from the genome did not lead to any obvious phenotype. Transaldolase was not produced in such mutants as shown by immunological detection. In combination with a double null-mutant in the genes encoding the phosphofructokinase subunits in K. lactis (Klpfk1 Klpfk2 Kltal1), the cells lost their ability to grow on glucose. We take this as strong evidence that glucose is metabolized via the pentose phosphate pathway in this yeast when glycolysis is blocked. In addition, by tetrad analysis we detected a close linkage to KIPFK1 and inferred that KITAL1 is localized on chromosome I.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb00957.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Specific gene probes as tools in yeast taxonomy (1985)
    Springer
    Current genetics 10 (1985), S. 103-110 
    Details
    ISSN: 1432-0983
    Keywords: Yeast taxonomy ; DNA homologies ; Southern analysis ; Glycolytic gene probes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The genePDC1 ofSaccharomyces cerevisiae coding for pyruvate decarboxylase (E.C. 4.1.1.1.) was used as a hybridization probe to detect gene sequence homologies in different strains ofSaccharomyces cerevisiae and in other yeast species. Additionally six other genes coding for glycolytic enzymes as well as the genesURA3 of the pyrimidine synthetic andTRP1 of the tryptophan synthetic pathways were used. A restriction polymorphism for the BamH1 fragments carrying thePDC1 gene was evident within the speciesSaccharomyces cerevisiae. All strains definitely declared asSaccharomyces cerevisiae showed the same restriction patterns. Hybridizations of different intensities were observed only with species in the familySaccharomycetaceae. Hybridizations with different genes showed different degrees of conservation for certain DNA sequences.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00636474
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Genetic and physiological evidence for the existence of a second glycolytic pathway in yeast parallel to the phosphofructokinase-aldolase reaction sequence (1984)
    Springer
    Molecular genetics and genomics 195 (1984), S. 536-540 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Yeast mutants lacking phosphofructokinase activity because of a defect in one of the two genes PFK1 and PFK2 can still perform glycolysis and produce ethanol. However, they differ from normal wild-type yeast in several ways. After a transfer from a sugar-free to a glucose medium, wild-type cells start to produce ethanol right away, mutants only after a lag period of about 90 min. About two-thirds of the carbon atoms released as CO2 from wild-type cells derive from glucose carbon atoms 3 and 4. Mutants with a single defect in one of the two phosphofructokinase genes PFK1 and PFK2 show no such a preferential contribution of these two C-atoms of glucose. All six C-atoms contribute almost equally to CO2 production. We have isolated mutants that block glycolysis in single pfk1 and pfk2 mutants. They could be located in three different genes called BYP1, BYP2 and BYP3 (BYP for bypass). In a byp1 mutant, CO2 derived almost exclusively from C-atoms 3 and 4 of glucose. This is what the classical concept of yeast glycolysis predicts. During a search for metabolites accumulating in pfk and byp mutants, we found sedoheptulose-7-phosphate, a pentosephosphate cycle intermediate not detectable in wild-type cells. An analysis of enzymes acting in the direct oxidation of glucose-6-phosphate and in the pentosephosphate cycle did not show any defects in those activities. It is hypothesized that the pentosephosphate cycle not only functions, in providing phosphorylated derivatives of tetroses and pentoses for biosynthetic needs, but also plays an important role in sugar catabolism and fermentation. This hypothesis also implies that the reaction sequency catalyzed by phosphofructokinase and aldolase covers only part of the total catabolic flux.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341459
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    A hybrid DNA sequence containing the replication origin of the multicopy yeast plasmid 2 μm circle and an additional repeated sequence can convert maltose-negative into maltose-positive strains (1984)
    Springer
    Molecular genetics and genomics 197 (1984), S. 491-496 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Yeast DNA pools were prepared by ligating partial Sau3A genomic digests from strains carrying various MAL genes into the BamHI site of the yeast-Escherichia coli shuttle vector YRp7. They were used to transform recipient yeast strains that could not utilize maltose since they lacked a classical MAL gene. Transformants were obtained that could use maltose and also formed normal levels of maltase. They were unstable. They would lose the selective marker TRP1 of YRp7 alone, together with the ability to utilize maltose or only the ability to utilize maltose. The insertion of one of the plasmids was used as a hybridization probe for the others and found to share homologous sequences with all. They were then shown to contain the replication origin of the yeast 2 μm circle plasmid and additional genomic digests of total yeast DNA. They hybridized at various degrees of efficiency with several bands, indicating that they were part of a family of repeated sequences. Apparently, it was the combination of the replication origin of the 2 μm circles with the additional sequences that promoted maltose utilization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00329948
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    A screen for upstream components of the yeast protein kinase C signal transduction pathway identifies the product of the SLG1 gene (1998)
    Springer
    Molecular genetics and genomics 258 (1998), S. 148-155 
    Details
    ISSN: 1617-4623
    Keywords: Key words Protein kinase C ; Signal transduction ; Transposon mutagenesis ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We employed the constitutive BCK1-20 allele of the gene for the MAP kinase kinase kinase (MAPKKK) in the yeast Pkc signal transduction pathway to develop a genetic screen for mutants in genes encoding upstream components. Transposon mutagenesis yielded a mutant that was completely dependent on the active allele in the absence of osmotic stabilization. The transposon had integrated at the yeast SLG1 (HCS77) locus. This gene encodes a putative membrane protein. Haploid slg1 deletion strains are sensitive to caffeine, as expected for mutants in the Pkc pathway, as well as a variety of other drugs. The response to elevated temperatures and the dependence on osmotic stabilization depends on the genetic background. Thus, in the strain used for mutagenesis, disruption of SLG1 causes the cells to become non-viable in the absence of osmotic stabilization at both 30° C and 37° C. In a different genetic background this phenotype was not observed. Sensitivity of the haploid deletion mutants to caffeine can be partially suppressed by overexpression of genes for other components of the Pkc pathway, such as PKC1, SLT2, ROM2, and STE20. In addition, a SLG1-lacZ reporter construct shows higher expression in the presence of caffeine or magnesium chloride in a wild-type diploid background.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050717
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Yeast mutants without phosphofructokinase activity can still perform glycolysis and alcoholic fermentation (1984)
    Springer
    Molecular genetics and genomics 195 (1984), S. 530-535 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants of Saccharomyces cerevisiae without detectable phosphofructokinase activity were isolated. They were partly recessive and belonged to two genes called PFK1 and PFK2. Mutants with a defect in only one of the two genes could not grow when they were transferred from a medium with a nonfermentable carbon source to a medium with glucose and antimycin A, an inhibitor of respiration. However, the same mutants could grow when antimycin A was added to such mutants after they had been adapted to the utilization of glucose. Double mutants with defects in both genes could not grow at all on glucose as the sole carbon source. Mutants with a single defect in gene PFK1 or PFK2 could form ethanol on a glucose medium. However, in contrast to wild-type cells, there was a lag period of about 2 h before ethanol could be formed after transfer from a medium with only nonfermentable carbon sources to a glucose medium. Wild-type cells under the same conditions started to produce ethanol immediately. Mutants with defects in both PFK genes could not form ethanol at all. Mutants without phosphoglucose isomerase or triosephosphate isomerase did not form ethanol either. Double mutants without phosphofructokinase and phosphoglucose isomerase accumulated large amounts of glucose-6-phosphate on a glucose medium. This suggested that the direct oxidation of glucose-6-phosphate could not provide a bypass around the phosphofructokinase reaction. On the other hand, the triosephosphate isomerase reaction was required for ethanol production. Experiments with uniformly labeled glucose and glucose labeled in positions 3 and 4 were used to determine the contribution of the different carbon atoms of glucose to the fermentative production of CO2. With only fermentation operating, only carbon atoms 3 and 4 should contribute to CO2 production. However, wild-type cells produced significant amounts of radioactivity from other carbon atoms and pfk mutants generated CO2 almost equally well from all six carbon atoms of glucose. This suggested that phosphofructokinase is a dispensable enzyme in yeast glycolysis catalyzing only part of the glycolytic flux.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341458
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Is the phosphofructokinase-reaction obligatory for glucose fermentation by Saccharomyces cerevisiae? (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 1 (1985), S. 173-175 
    Details
    ISSN: 0749-503X
    Keywords: Phosphofructokinase ; glycolysis ; alternative pathway(s) ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320010205
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Obituary: In Memory of Michael Ciriacy (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 881-882 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No Abstract
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...