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  • Articles: DFG German National Licenses  (7)
  • Electronic Resource  (7)
  • 1995-1999  (2)
  • 1990-1994  (5)
  • 1
    Electronic Resource
    Electronic Resource
    The purine-cytosine permease gene of Saccharomyces cerevisiae: primary structure and deduced protein sequence of the FCY2 gene product (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A 2.1 kb DNA segment carrying the purine-cytosine permease gene (FCY2) of Saccharomyces cerevisiae was sequenced, the primary structure of the protein (533 amino acids) deduced and a folding pattern in the membrane is proposed for the permease protein. Expression of the FCY2 gene product requires a functional secretory pathway and is reduced in mnn9, a mutant strain deficient in outer chain glycosylation. The FCY2 gene was mapped on the right arm of chromosome V close to the HIS1 gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1990.tb00627.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of a specific region of the purine–cytosine permease involved in the recognition of its substrates (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Three u.v.-induced mutants of the purine–cytosine permease gene of Saccharomyces cerevisiae, with altered apparent Michaelis constant of transport (Kmapp), were cloned and sequenced. One of the mutants had extensive nucleotide replacement, whereas the other two had a single mutation. To evaluate the contribution of the different amino acid replacements to the phenotype of the complex mutant, simpler mutants were created by site-directed mutagenesis. All the amino acid replacements found in the segment from amino acids 371 to 377 inclusive, contribute to the determination of the phenotype. According to the model postulated this segment lies on the cell surface. In particular, amino acids at position 374 and 377 modulate the affinity of the permease towards its substrates. In the wild-type, when asparagine is present at both of these positions, the lowest Kmapp values are found.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb01757.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Transport properties of a C. albicans amino-acid permease whose putative gene was cloned and expressed in S. cerevisiae (1993)
    Springer
    Current genetics 24 (1993), S. 487-490 
    Details
    ISSN: 1432-0983
    Keywords: Amino-acid permease ; Heterologous complementation ; Candida albicans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using a gene bank of C. albicans, the lysine-permease deficiency in a strain of S. cerevisiae was complemented, and the restriction map of the corresponding C. albicans DNA fragment was constructed. Its expression in S. cerevisiae showed that the permease of C. albicans actively transports arginine (KT=18 μmol/l, Jmax=26 nmol/min per mg dry weight), lysine (KT=12 μmol/l, Jmax=18 nmol/min per mg dry weight), histidine (KT=37 μmol/l, Jmax=9.7 nmol/min per mg dry weight), as well as their toxic analogues canavanine and thialysine, with high affinity. The intracellular concentration of basic amino acids transported into S. cerevisiae by the C. albicans permease reaches more than a thousand-times-higher value compared to the external concentration in the medium. Accumulated amino acids do not leave the cells. The uptake is strongly reduced by the protonophores and inhibitors of plasma membrane H+-ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351710
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  • 4
    Electronic Resource
    Electronic Resource
    Thialysine-resistant mutants and uptake of lysine in Schizosaccharomyces pombe (1992)
    Springer
    Current genetics 21 (1992), S. 351-355 
    Details
    ISSN: 1432-0983
    Keywords: Schizosaccharomyces pombe ; Thialysine resistance ; Lysine transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants defective in lysine transport were isolated and characterized. After UV-mutagenesis colonies resistant to thialysine, a toxic analogue of lysine, were isolated and L-lysine uptake into the mutant strains was analyzed. Among the thialysine-resistant strains a group of mutants was found, where the half-saturation constant, KT, of the high-affinity transport system for lysine was higher than in the wild-type, the high-affinity transport system for basic amino acids being specifically affected. This was confirmed by a complementation test in which all the thialysine-resistant strains with a higher KT for lysine uptake belonged to one complementation group. Kinetic and genetic analysis showed that our mutants were identical with can1-1 mutants, showing that a single high-affinity system for the transport of basic amino acids exists in S. pombe.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351694
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    The uracil permease of Schizosaccharomyces pombe: A representative of a family of 10 transmembrane helix transporter proteins of yeasts (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 1051-1059 
    Details
    ISSN: 0749-503X
    Keywords: Schizosaccharomyces pombe ; Saccharomyces cerevisiae ; uracil permease ; transmembrane helices ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The uracil permease gene of Schizosaccharomyces pombe was cloned and sequenced. The deduced protein sequence shares strong similarities with five open reading frames from Saccharomyces cerevisiae, namely the uracil permease encoded by the FUR4 gene, the allantoin permease encoded by DAL4, a putative uridine permease (YBL042C) and two unknown ORFs YOR071c and YLR237w.A topological model retaining ten transmembrane helices, based on predictions and on experimental data established for the uracil permease of S. cerevisiae by Galan and coworkers (1996), is discussed for the four closest proteins of this family of transporters. The sequence of the uracil permease gene of S. pombe has been deposited in the EMBL data bank under Accession Number X98696. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 6
    Electronic Resource
    Electronic Resource
    The immunodetected yeast purine - cytosine permease is not N-linked glycosylated, nor are glycosylation sequences required to have a functional permease (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 15-23 
    Details
    ISSN: 0749-503X
    Keywords: Purine-cytosine permease ; S. cerevisiae ; N-linked glycosylation ; immunoprecipitation ; site-directed mutagenesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The purine-cytosine permease (PCP) of the yeast Saccharomyces cerevisiae was detected by immunological methods. Using antibodies directed against synthetic peptides, whose sequences were derived from the primary structure of the PCP, immunoprecipitation of [35S]methionine-labelled PCP was achieved either from cellular extracts or from in vitro translation mixtures. Non-labelled PCP was also detected on Western blots of membrane proteins. Similar migration rates were observed for PCP originating both from immunoprecipitated cellular extracts and from in vitro translation mixtures. Hence, post-translational processing, if any, only slightly affects the size of the protein. Also no evidence was found for N-linked core-glycosylation: identical migration rates were observed when immunoprecipitated PCP molecules were extracted from cells labelled for 10 min with [35S]methionine, pretreated or not with tunicamycin.On the other hand, the suppresion of the two potential N-linked glycosylation sequences in the DNA did not lead to inactivation of the transport activity, confirming that N-linked glycosylation is not required for the permease activity.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110103
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  • 7
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding for a lysine-specific permease (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 771-782 
    Details
    ISSN: 0749-503X
    Keywords: Lysine transport ; permease ; S. cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The LYP1 gene of Saccharomyces cerevisiae was cloned by complementation in lysine-permease-deficint recipient yeast cells, and its nucleotide sequence was determined. An open reading frame of 1833 nucleotides was found encoding a polypeptide of 611 amino acids, with a calculated molecular weight of 68 118. Analysis of the deduced primary structure of the protein revealed ten membrane-spanning regions and three potential N-glycosylation sites. Analysis of the deduced sequence of protein LYP1 indicates homology with other yeast amino-acid permeases, in particular with CAN1, and also the lysine-specific permease of Escherichia coli. The strain transformed by a multi-copy plasmid harbouring the LYP1 gene, showed a 20-fold increase in the maximum velocity of lysine uptake over that in the wild type, with no changes in the affinity of the permease for its substrate.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090711
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    Paper (German National Licenses)
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