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  • 1
    Electronic Resource
    Electronic Resource
    6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae (1992)
    Springer
    Current genetics 22 (1992), S. 9-11 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; IMP dehydrogenase ; 6-azauracil ; GTP level
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The addition of 6-azauracil to the growth medium causes a strong reduction of the GTP level in the nucleotide pool of Saccharomyces cerevisiae. In-vitro experiments show a strong inhibition of IMP dehydrogenase activity by 6-azaUMP explaining the preceeding effect. PPR2 mutants, previously characterized by an increased sensitivity to 6-azauracil compared to the wildtype, are specifically susceptible to the lowering of the GTP pool, and are able to grow in presence of 6-azauracil when guanine is added to the medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351735
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning of an Arabidopsis thaliana cDNA coding for farnesyl diphosphate synthase by functional complementation in yeast (1994)
    Springer
    Plant molecular biology 26 (1994), S. 1867-1873 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; cDNA ; complementation ; erg20-2 yeast mutant ; farnesyl diphosphate synthase ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA encoding farnesyl diphosphate synthase, an enzyme that synthesizes C15 isoprenoid diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate, was cloned from an Arabidopsis thaliana cDNA library by complementation of a mutant of Saccharomyces cerevisiae deficient in this enzyme. The A. thaliana cDNA was also able to complement the lethal phenotype of the erg20 deletion yeast mutant. As deduced from the full-length 1.22 kb cDNA nucleotide sequence, the polypeptide contains 343 amino acids and has a relative molecular mass of 39689. The predicted amino acid sequence presents about 50% identity with the yeast, rat and human FPP synthases. Southern blot analyses indicate that A. thaliana probably contains a single gene for farnesyl diphosphate synthase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019499
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning, sequencing and characterization of the Saccharomyces cerevisiae URA7 gene encoding CTP synthetase (1991)
    Springer
    Molecular genetics and genomics 231 (1991), S. 7-16 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; CTP synthetase ; Pyrimidine pathway ; Intracellular pyrimidine pool ; Non-essential gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The URA7 gene of Saccharomyces cerevisiae encodes CTP synthetase (EC 6.3.4.2) which catalyses the conversion of uridine 5′-triphosphate to cytidine 5′-triphosphate, the last step of the pyrimidine biosynthetic pathway. We have cloned and sequenced the URA 7 gene. The coding region is 1710 by long and the deduced protein sequence shows a strong degree of homology with bacterial and human CTP synthetases. Gene disruption shows that URA7 is not an essential gene: the level of the intracellular CTP pool is roughly the same in the deleted and the wild-type strains, suggesting that an alternative pathway for CTP synthesis exists in yeast. This could involve either a divergent duplicated gene or a different route beginning with the amination of uridine mono- or diphosphate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293815
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  • 4
    Electronic Resource
    Electronic Resource
    Use of synthetic lethal mutants to clone and characterize a novel CTP synthetase gene in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 431-439 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Duplicate genes ; Synthetic lethal mutants ; CTP synthetase ; Pyrimidine biosynthetic pathway
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the pyrimidine biosynthetic pathway, CTP synthetase catalyses the conversion of uridine 5′-triphosphate (UTP) to cytidine 5′-triphosphate (CTP). In the yeast Saccharomyces cerevisiae, the URA7 gene encoding this enzyme was previously shown to be nonessential for cell viability. The present paper describes the selection of synthetic lethal mutants in the CTP biosynthetic pathway that led us to clone a second gene, named URA8, which also encodes a CTP synthetase. Comparison of the predicted amino acid sequences of the products of URA7 and URA8 shows 78% identity. Deletion of the URA8 gene is viable in a haploid strain but simultaneous presence of null alleles both URA7 and URA8 is lethal. Based on the codon bias values for the two genes and the intracellular concentrations of CTP in strains deleted for one of the two genes, relative to the wild-type level, URA7 appears to be the major gene for CTP biosynthesis. Nevertheless, URA8 alone also allows yeast growth, at least under standard laboratory conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281793
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  • 5
    Electronic Resource
    Electronic Resource
    Heterospecific cloning of Arabidopsis thaliana cDNAs by direct complementation of pyrimidine auxotrophic mutants of Saccharomyces cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the second, fifth and sixth steps of the de novo pyrimidine biosynthesis pathway (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 23-32 
    Details
    ISSN: 1617-4623
    Keywords: Arabidopsis thaliana ; Saccharomyces cerevisiae ; Complementation ; Aspartate transcarbamylase ; Orotate phosphoribosyl transferase ; Orotidine-5′-phosphate decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An Arabidopsis thaliana cDNA library was used to complement Saccharomyces cerevisiae pyrimidine auxotrophic mutants. Mutants in all but one (carbamylphosphate synthetase) of the six steps in the de novo pyrimidine biosynthetic pathway could be complemented. We report here the cloning, sequencing and computer analysis of two cDNAs encoding the aspartate transcarbamylase (ATCase; EC 2.1.3.2) and orotate phosphoribosyltransferase-orotidine-5′-phosphate decarboxylase (OPRTase-OMP-decase; EC 2.4.2.10, EC 4.1.1.23) enzymes. These results confirm the presence in A. thaliana of a bifunctional gene whose product catalyses the last two steps of the pyrimidine biosynthetic pathway, as previously suggested by biochemical studies. The ATCase encoding cDNA sequence (PYRB gene) shows an open reading frame (ORF) of 1173 by coding for 390 amino acids. The cDNA encoding OPRTase-OMPdecase (PYRE-F gene) shows an ORF of 1431 by coding for 476 amino acids. Computer analysis of the deduced amino acid sequences of both cDNAs shows the expected high similarity with the ATCase, ornithine transcarbamylase (OTCase; EC 2.1.3.3), OPRTase and OMPdecase families. This heterospecific cloning approach increases our understanding of the genetic organization and interspecific functional conservation of the pyrimidine biosynthetic pathway and underlines its usefulness as a model for evolutionary studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280183
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  • 6
    Electronic Resource
    Electronic Resource
    Construction of a Yeast Strain Deleted for the TRP1 Promoter and Coding Region that Enhances the Efficiency of the Polymerase Chain Reaction-Disruption Method (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 353-356 
    Details
    ISSN: 0749-503X
    Keywords: TRP1 ; one-step deletion method ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The sequence of the genome of Saccharomyces cerevisiae was recently determined. As well as all the information concerning the structure of the chromosomes the scientific community had to deal with the discovery of dozens of new open reading frames (ORFs) of unknown function. The study of these ORFs requires the development of simple procedures that can be used on a large scale. In the framework of a European Pilot Project we have described a new approach for deleting ORFs. This method is based on transformation with a polymerase chain reaction product but is limited by the use of a strain deleted for the auxotropic marker. We present here the construction of a new recipient strain that lacks the TRP1 region and that allows a high efficiency of gene deletion. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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