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  • 1
    Electronic Resource
    Electronic Resource
    As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe (1995)
    Springer
    Current genetics 28 (1995), S. 138-149 
    Details
    ISSN: 1432-0983
    Keywords: Schizosaccharomyces pombe ; Pyrimidine pathway ; Feedback inhibition ; DHOase-like ; Multifunctional protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The organisation of the URA1 gene of Schizosaccharomyces pombe was determined from the entire cDNA cloned by the transformation of an ATCase-deficient strain of Saccharomyces cerevisiae. The URA1 gene encodes the bifunctional protein GLNase/CPSase-ATCase which catalyses the first two steps of the pyrimidine biosynthesis pathway. The complete nucleotide sequence of the URA1 cDNA was elucidated and the deduced amino-acid sequence was used to define four domains in the protein; three functional domains, corresponding to GLNase (glutamine amidotransferase), CPSase (carbamoylphosphate synthetase) and ATCase (aspartate transcarbamoylase) activities, and one cryptic DHOase (dihydroorotase) domain. Genetic investigations confirmed that both GLNase/CPSase and ATCase activities are carried out by the same polypeptide. They are also both feedback-inhibited by UTP (uridine triphosphate). Its organization and regulation indicate that the S. pombe URA1 gene product appears very similar to the S. cerevisiae URA2 gene product.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315780
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  • 2
    Electronic Resource
    Electronic Resource
    Mutations in STS1 suppress the defect in 3′ mRNA processing caused by the rna15-2 mutation in Saccharomyces cerevisiae (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 552-562 
    Details
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; mRNA 3′ processing ; Poly(A) tail ; STS1 ; RNA15
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  In a search for proteins associated with Rna15p in processing the 3′ ends of messenger RNAs, we have looked for suppressors that correct, even partially, the thermosensitive growth defect of the rna15-2 mutant. Mutations in a single locus that we named SSM5, were able to suppress both the thermosensitivity of cell growth and the mRNA 3′ processing defect associated with the rna15-2 mutation, but only slightly alleviated the thermosensitive growth defect of an rna14-1 mutant. The ssm5-1 mutant is sensitive to hydroxyurea at 37° C, a drug that inhibits DNA synthesis. By screening for complementation of the hydroxyurea-sensitive phenotype we cloned the corresponding wild-type gene and found that it corresponds to the essential gene STS1 (also named DBF8). Sts1p has an apparent molecular weight of 30 kDa and was confirmed to be a cytosolic protein by immunofluorescence analysis. Western blot analysis indicates that the thermosensitive mutant strains rna15-2, rna14-1 and pap1-1 present a very low level of the Rna15p at 37° C. The ssm5-1 mutation restores the level of Rna15p in the rna15-2 ssm5-1 double mutant. Use of the two-hybrid system suggests that Sts1p does not interact directly with Rna15p, but may be active as a homodimer. The present data suggest that Sts1p may play a role in the transport of Rna15p from the cytoplasm to the nucleus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172401
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  • 3
    Electronic Resource
    Electronic Resource
    SLS1, a new Saccharomyces cerevisiae gene involved in mitochondrial metabolism, isolated as a syntheticlethal in association with an SSM4 deletion (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 700-708 
    Details
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; Mitochondria ; Integral membrane protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  SSM4 was isolated as a suppressor of rna14-1, a mutant involved in nuclear mRNA maturation. In order to isolate genes interacting with SSM4, we have searched for mutants that are syntheticlethal in association with an SSM4 deletion. Among the mutants obtained, one, named sls1-1, shows a pet - phenotype. We have cloned and sequenced this gene. It encodes a protein with a calculated molecular mass of 73 kDa. This protein contains a mitochondrial targeting pre-sequence but does not show homology with other known proteins. Deletion of SLS1 does not affect cell viability on glucose but is lethal on a non-fermentable medium. The Sls1p protein does not appear to be involved in mitochondrial DNA replication, transcription, or in RNA splicing maturation or stability. We have also tagged this protein and localized it in mitochondria. Treatment with alkaline carbonate does not extract this protein from mitochondria, suggesting strongly that it is a mitochondrial integral membrane protein. Thus, the SLS1 gene, encodes a mitochondrial integral membrane protein and is paradoxically synlethal in association with a deletion of the SSM4 gene, which encodes an integral nuclear membrane protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173976
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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae (1990)
    Springer
    Current genetics 18 (1990), S. 287-291 
    Details
    ISSN: 1432-0983
    Keywords: Purine biosynthesis ; Yeasts ; HeLa ; cDNA library
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A HeLa cell cDNA library on a yeast expression vector was used to complement auxotrophic markers of Saccharomyces cerevisiae. Clones complementing the ade2-101 mutation harbor a 1.5 kb poly(A)+ tailed insert with a 425 amino acid open reading frame hybridizing with two human mRNAs of 1.5 kb and 3.1 kb. Its 5′ half is homologous to Bacillus subtilis SAICAR synthetase (E.C.6.3.2.6.) and its 3′ terminal half corresponds to the catalytic subunit of Escherichia coli and B. subtilis AIR carboxylase (E.C.4.1.1.21). In agreement with these homologies, pADE2H1 clones complement both ade1 and ade2 mutants of S. cerevisiae, as was also recently reported for a 3.1 kb cDNA isolated from human hepatocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318209
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of ochre nonsense mutations on yeast URA1 mRNA stability (1984)
    Springer
    Current genetics 8 (1984), S. 277-282 
    Details
    ISSN: 1432-0983
    Keywords: mRNA stability ; Nonsense mutant ; Eukaryotic transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The genetic map of 27 mutants of the URA1 yeast gene has been established by meiotic recombination and 16 nonsense mutations characterized. The half life of URA1 mRNA was determined by two independent methods in the wild-type and in two ochre mutants localized at each extremity of the genetic map. A halflife of 15 min was found for the wild-type and for one of the ochre mutants. This half-life was radically reduced in the other ochre mutant whereas the instantaneous rate of its mRNA synthesis remained constant. After subcloning various endonucleolytic fragments the coding sequence of the URA1 gene was restricted to a 1.65 kb fragment within a 5.7 kb yeast DNA segment. Direct visualization of the URA1 mRNA by Northern hybridization of denatured RNA with a URA1 specific DNA probe revealed a length of 1.5 kb.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419725
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  • 7
    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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  • 8
    Electronic Resource
    Electronic Resource
    RNA and protein elongation rates in Saccharomyces cerevisiae (1973)
    Springer
    Molecular genetics and genomics 125 (1973), S. 319-327 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The RNA elongation rate has been measured in yeast by the kinetics of appearance of radioactivity in the different molecular weight classes by the method first developed by Bremer and Yuan (1968). Despite the limitations caused by the breakdown of the 35s rRNA precursor, an estimate of 29 to 38 nucleotides/second at 30° has been obtained for the RNA elongation rate. The protein elongation rate has been calculated by the method of Maaløe and Kjeldgaard (1966) which consists of dividing the number of amino acids polymerized into protein per unit of time by the number of active ribosomes. This has given values of 7 to 9 amino acids/second at 30°. These numbers are of the same order as those found in Escherichia coli when corrected to 37°. Eucaryotic cells could thus have preserved part of the coupling found in bacteria between RNA and protein elongation rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276587
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  • 9
    Electronic Resource
    Electronic Resource
    Fine structure of the ura 2 locus in Saccharomyces cerevisiae (1971)
    Springer
    Molecular genetics and genomics 112 (1971), S. 354-364 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Studies of complementation patterns of ura2 mutants of the pyrimidine pathway in Saccharomyces cerevisiae suggest the existence of at least two different structural genes in the ura2 locus: one coding for carbamyl phosphate synthetase, ura2C and the other coding for aspartic transcarbamylase, ura2A. An interallelic type of complementation takes place among some ura2A mutants, but was not noted among the ura2C class (Fig. 2). Preliminary results of the mapping of suppressible mutants indicate that the complex is transcribed into a single messenger RNA, with the direction of transcription proceeding from the CPSase region to the ATCase region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334436
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  • 10
    Electronic Resource
    Electronic Resource
    Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast (1975)
    Springer
    Molecular genetics and genomics 136 (1975), S. 327-335 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary [URE3], a non-mitochondrial non-mendelian mutation which modifies drastically yeast nitrogen metabolism has been genetically studied. Cytoduction experiments show definitely that the inheritance of the determinant is not linked to the nucleus. The maintenance of the [URE3] determinant seems controlled by the product of a conventional nuclear gene (ure2) which is itself involved in nitrogen metabolism. The (ure2) mutation alone gives the same phenotype as [URE3] but it is impossible to obtain a stable recombinant containing simultaneously the (ure2) mutation and the [URE3] determinant. Application of the Newcombe respreading experiment demonstrates that the [URE3] mutational event occurs before the selection procedure and is therefore not strictly adaptative. Nevertheless, the nature of the selection medium changes considerably the frequency of the [URE3] mutants recovered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341717
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