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  • 1
    Electronic Resource
    Electronic Resource
    Aspergillus oryzae produces compounds inhibiting cholesterol biosynthesis downstream of dihydrolanosterol (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 242 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The formation of cholesterol synthesis inhibiting molecules by five different strains of the koji mold Aspergillus oryzae was studied. After growing these strains on a complex liquid medium we found in crude organic phase extracts and specific fractions there from compounds inhibiting cholesterol synthesis in human hepatic T9A4 cells in vitro at enzyme sites downstream of dihydrolanosterol. This was evidenced by using different radioactively labeled precursors, namely acetate, mevalonate, 24,25-dihydro-[24,25-3H2]-lanosterol or [3-3H]-lathosterol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2004.11.001
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  • 2
    Electronic Resource
    Electronic Resource
    By-product formation during exposure of respiring Saccharomyces cerevisiae cultures to excess glucose is not caused by a limited capacity of pyruvate carboxylase (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 179 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Upon exposure to excess glucose, respiring cultures of Saccharomyces cerevisiae produce substantial amounts of ethanol and acetate. A possible role of a limited anaplerotic capacity in this process was investigated by overexpressing pyruvate carboxylase and by replacing it with a heterologous enzyme (Escherichia coli phosphoenolpyruvate carboxylase). Compared to the wild-type, neither the pyruvate carboxylase (Pyc)-overexpressing nor the transgenic strain exhibited reduced by-product formation after glucose pulses to aerobic glucose-limited chemostat cultures. An increased intracellular malate concentration was observed in the two engineered strains. It is concluded that by-product formation in S. cerevisiae is not caused by a limited anaplerotic capacity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb08715.x
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  • 3
    Electronic Resource
    Electronic Resource
    Identification and characterization of four new GCD genes in Saccharomyces cerevisiae (1986)
    Springer
    Current genetics 10 (1986), S. 657-664 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Amino acid biosynthesis ; General control ; GCD-genes ; GCN-genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutant strains, resistant against the amino acid analogues 5-methyltryptophan, 5-fluorotryptophan and canavanine were isolated, starting with a trp2 leaky auxotrophic strain. Of 10 such strains, only four turned out to be of the “general control derepressed” (gcd) mutant type. Three other isolates were shown to be defective in the general amino acid permease system, while the remaining three strains displayed low spore viability and were not further investigated. Complementation tests amongst the four new gcd-mutant strains, including strain RH558 gcd2-1 isolated earlier, yielded five complementation groups: GCD2, GCD3, GCD4, GCD5, and GCD6. All mutant strains showed a dual phenotype, which was not separable by wild type backcrosses: “constitutive derepression” and “slow growth”. Epistatis of all gcd mutations over gcn1-1, gcn2-1 and gcn3-1 was found with respect to both phenotypes, except for gcd5-1, which was lethal in these combinations. On the other hand gcn4-101 was found to be epistatic over all gcd mutations, but only with respect to the “constitutive derepression” phenotype, and not to “slow growth”; again the combination with gcd5-1 was lethal. Mutation gcd2-1 was mapped on chromosome VII, 50 cM from leu1 and 22 cM from ade6. A new model is discussed, in which GCD-genes are involved in the amino acid uptake into the vacuoles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410913
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  • 4
    Electronic Resource
    Electronic Resource
    Structure and function of the TRP3 gene of Saccharomyces cerevisiae: Analysis of 3′- and 5′-deletions in vivo and in vitro (1984)
    Springer
    Current genetics 8 (1984), S. 173-180 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; TRP3 gene ; Deletion analysis ; Enzyme function
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two sets of deletions, entering the TRP3 gene of Saccharomyces cerevisiae from the 3′- and the 5′-end were constructed. Complementation analysis with chromosomal trp3A, trp3B and trp3C mutations was done by introducing the 3′- and 5′-truncated gene on a multicopy 2 μm-vector. The N-terminal glutamine amido transferase function is encoded by a DNA fragment of 600–700 bp, and the C-terminal indole-3-glycerol-phosphate synthase function by a DNA fragment of about 900 bp, whereas both functions together are encoded by a contiguous DNA fragment of about 1,500 bp. The bi functional TRP3-peptide thus could be dissected into two catalytically independent peptides in vivo. For the indole-3-glycerol-phosphate synthase activity, independent catalytic activity was also demonstrated in vitro: deletions entering the TRP3 gene from the 5′-end, and lacking large parts of the sequence coding for the glutamine amidotransferase function, still are able to ex press a peptide exhibiting functional indole-3-glycerol phosphate synthase activity in vitro. Deletion plasmids pME505·De1C102·2μm and DelC10·2μm exhibited shorter TRP3 transcripts according to the deleted DNA-fragments (150 and 426 by respectively) but yielded peptides of invariable Mr of 35,000 d. Transcription and translation of these peptides, which probably represent the independently folding indole-3-glycerol-phosphate synthase core are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00417813
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation of the TRP2 and the TRP3 genes of Saccharomyces cerevisiae by functional complementation in yeast (1982)
    Springer
    Current genetics 5 (1982), S. 39-46 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; TRP2 gene ; TRP3 gene ; Cloning in yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary This paper describes the isolation of the TRP2 and the TRP3 genes of Saccharomyces cerevisiae. Two pools of plasmids consisting of BamHI and Sa1GI yeast DNA inserts into the bifunctional yeast — Escherichia coli vector pLC544 (Kingsman et al. 1979) were constructed in E. coli and used for the isolation of the two genes by selection for functional complementation of trp2 and trp3 mutations, respectively, in yeast. The TRP2 gene was isolated on a 6.2 kb BamHl and a 5.8 kb Sa1GI yeast DNA fragment which shared an identical 4.5 kb BamHI-SaIGI fragment. The TRP3 gene was located on a 5.2 kb BamHl fragment. By physical, genetic and physiological experiments it could be shown that the cloned yeast DNA fragments contained the whole structural sequences as well as the regulatory regions of the TRP2 and the TRP3 genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00445739
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  • 6
    Electronic Resource
    Electronic Resource
    Structure and function of the TRP3 gene of Saccharomyces cerevisiae: Analysis of transcription, promoter sequence, and sequence coding for a glutamine amidotransferase (1984)
    Springer
    Current genetics 8 (1984), S. 165-172 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; TRP3 gene ; Sequence analysis ; Enzyme function
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The structure and function of the TRP3 gene of Saccharomyces cerevisiae were analyzed. Subcloning of an original 4.8 kb BamHI DNA fragment, carrying the yeast TRP3 gene, allowed for a localization of the gene on a 2.5 kb ClaI/BamHI fragment. Transcription was found to proceed from the ClaI site towards the BamHI site. Three major transcription start sites were determined at positions −92, −87, and −81 by S1-mapping. The synthesis of the TRP3 gene is regulated by the general control, and was found to take place- at the transcriptional level. The sequence of the 5′-noncoding region up to position −400 and part of the coding region to position 840 were determined. The 5′-noncoding region contains sequences common to most amino acid biosynthetic genes known so far, namely a presumptive ribosome binding site, “Goldberg-Hogness boxes”, and a consensus sequence, possibly involved in the general control. For the coding region a single open reading frame was found. The deduced amino acid sequence was aligned with homologous amino acid sequences of Neurospora crassa, Pseudomonas putida and Escherichia coli. The exceptionally high homology (40–60%) between these sequences led us to postulate that the TRP3 gene product is of the structure NH2-glutamine amidotransferase-indole-3-glycerol-phosphate synthase-COOH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00417812
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  • 7
    Electronic Resource
    Electronic Resource
    Arrangement of genes TRP1 and TRP3 of Saccharomyces cerevisiae strains (1985)
    Springer
    Archives of microbiology 142 (1985), S. 383-388 
    Details
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Tryptophan biosynthesis ; General control ; Systematic by Southern hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The tryptophan biosynthetic genes TRP1 and TRP3 and partly also TRP2 and TRP4 have been compared by the technique of Southern hybridization and enzyme measurements in twelve wild isolates of Saccharomyces cerevisiae from natural sources of different continents, in the commonly used laboratory strain S. cerevisiae X2180-1A and in a Kluyveromyces marxianus strain. We could classify these strains into four groups, which did not correlate with their geographical distribution. In no case are the TRP3 and TRP1 genes fused as has been found in other ascomycetes. Two strains were found which, in contrast to strain X2180-1A, show derepression of gene TRP1. Two examples are discussed to demonstrate the usefulness of Southern hybridizations for the identification of closely related strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00491908
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  • 8
    Electronic Resource
    Electronic Resource
    Inhibition of yeast tRNATrp aminoacylation by 4-methyltryptophan (1981)
    Springer
    Archives of microbiology 129 (1981), S. 146-149 
    Details
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Inhibition of tryptophanyl-tRNA synthetase ; Mode of action of tryptophan analogues ; Tryptophan analogue degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of the tryptophan analogue 4-methyltryptophan in Saccharomyces cerevisiae has been investigated. 4-Methyltryptophan inhibits the aminoacylation of tryptophan specific transfer ribonucleic acid (tRNATrp). The mode of inhibition is competitive and the analogue is not charged onto tRNATrp. Thus 4-methyltryptophan application depletes the cells from charged tRNATrp. As a consequence cell growth and protein synthesis are strongly reduced. 4-Methyltryptophan is degraded efficiently in culture media inoculated with the wild type strain; the effects of 4-methyltryptophan were therefore found to be transient.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00455351
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  • 9
    Electronic Resource
    Electronic Resource
    Action of tryptophan analogues in Saccharomyces cerevisiae (1977)
    Springer
    Archives of microbiology 115 (1977), S. 307-316 
    Details
    ISSN: 1432-072X
    Keywords: Anthranilate synthase, feedback inhibition of ; Saccharomyces cerevisiae ; Tryptophan analogues, mode of action of ; Tryptophan biosynthetic enzymes ; Tryptophan pool
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In an analysis of the effects of various tryptophan and indole analogues in Saccharomyces cerevisiae we determined the mechanisms by which they cause growth inhibition: 4-Methyltryptophan causes a reduction in protein synthesis and a derepression of the tryptophan enzymes despite of the presence of high internal levels of tryptophan. This inhibition can only be observed in a mutant with increased permeability to the analogue. These results are consistent with but do not prove an interference of this analogue with the charging of tryptophan onto tRNA. 5-Methyltryptophan causes false feedback inhibition of anthranilate synthase, the first enzyme of the tryptophan pathway. This inhibits the further synthesis of tryptophan and results in results in tryptophan limitation, growth inhibition and derepression of the enzymes. Derepression eventually allows wild type cells to partially overcome the inhibitory effect of the analogue. 5-Fluoroindole is converted endogenously to 5-fluorotryptophan by tryptophan synthase. Both endogenous and externally supplied 5-fluorotryptophan are incorporated into protein. This leads to intoxication of the cells due to the accumulation of faulty proteins. 5-Fluorotryptophan also causes feedback inhibition of anthranilate synthase and reduces the synthesis of tryptophan which would otherwise compete with the analogues in the charging reaction. Indole acrylic acid inhibits the conversion of indole to tryptophan by tryptophan synthase. This results in a depletion of the tryptophan pool which, in turn, causes growth inhibition and derepression of the tryptophan enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446457
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of an artificial yeast TRP-gene cluster in yeast and Escherichia coli (1984)
    Springer
    Molecular genetics and genomics 195 (1984), S. 481-486 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary All five tryptophan biosynthetic genes of Saccharomyces cerevisiae were unified on plasmid pME554, which is based on 2 μm DNA and pBR322 sequences allowing for autonomous replication in yeast and E. coli. Homologous and heterologous expression of this artificial yeast TRP-gene cluster was studied. Plasmid pME554 allowed for nearly normal growth of a yeast strain bearing auxotrophic mutations in all five TRP-genes. The plasmid-borne genes TRP2 to TRP5 were expressed and regulated normally in the frame of the general control. Gene TRP1, carried on an EcoRI/BglII fragment lacking the ARS1 function, was expressed poorly and did not respond to the general control like the chromosomally-borne TRP1 gene. Plasmid pME554 allowed for poor growth of E. coli strain W3110 tna − ΔtrpEA2 on minimal medium. Marked stimulation was observed, however, when anthranilic acid or indole were added. Accordingly, poor expression of the first Trp-enzyme anthranilate synthase and the last enzyme tryptophan synthase was found, whereas the other three genes were moderately well expressed in E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341450
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