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  • 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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  • 2
    Electronic Resource
    Electronic Resource
    Genetic Diversity of the Date Palm (Phoenix dactylifera L.) from Algeria Revealed by Enzyme Markers (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Plant breeding 107 (1991), S. 0 
    Details
    ISSN: 1439-0523
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Analysis of the enzymatic polymorphism of the date palm, Phoenix dactylifera L., was undertaken to evaluate the genetic variability of Algerian cultivars. Seven enzyme systems (alcohol dehydrogenase, diaphorase, aspartate aminotransaminase, acid phosphatase, endopeptidase, leucine aminopeptidase and phosphoglucomutase) were visualized by electrophoresis. Genetic hypotheses appear to show 7 polymorphic loci and 16 alleles were counted. The study of diversity showed a high percentage of polymorphic loci, strong heterozygosity and considerable genetic diversity. The study shows that genetic variability is greater in the cultivars in the western regions (Saoura-Touat) than in the eastern regions (Rhir-Zibans). An identification key was devised and nearly 65% of the cultivars studied were identified from 5 enzyme systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1439-0523.1991.tb00528.x
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  • 3
    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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  • 4
    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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  • 5
    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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  • 6
    Electronic Resource
    Electronic Resource
    Cell populations in the lesion of human cutaneous leishmaniasis: A light microscopical, immunohistochemical and ultrastructural study (1992)
    Springer
    Virchows Archiv 421 (1992), S. 239-247 
    Details
    ISSN: 1432-2307
    Keywords: Human cutaneous leishmaniasis ; Skin ; Immunohistochemistry ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To characterize the in situ cellular immune response in localized cutaneous leishmaniasis (LCL), the authors studied frozen skin biopsies from 50 patients with LCL due toLeishmania braziliensis guyanensis. A panel of 31 monoclonal antibodies was used, which defined the number and distribution of inflammatory cell subsets. Skin inflammatory infiltrates were composed of T cells (with a local CD4/CD8 ratio of 1.05±0.7 vs 1.48±0.3 in peripheral blood), macrophages and a smaller number of B cells, natural killer cells and granulocytes. Most of the T cells expressed activation markers (interleukin-2 and transferrin receptors, HLA-DR+) and an increase in T-cell-receptorγδ expression was noted. Analysis of the CD4+ subpopulations with newly available reagents showed that helper T cells (CD4+CD45RO+) exceeded the suppressor/inducer subset (CD4+CD45RA+) by 1.4∶1. There were no differences between local immune variables from patients with primary infection (45 patients) and those with recurrence (5). In 7 patients, biopsies were analysed before and 1 month after specific treatment, and did not show significant differences except for a small increase of dermal CD1a+ (Langerhans) cells/mm2. The observed pattern of cellular skin infiltration suggests an immune-mediated tissue injury including T-cell-mediated cytotoxicity and delayed hypersensitivity reactions in addition to direct parasitic action.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01611181
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  • 7
    Electronic Resource
    Electronic Resource
    Genetic diversity among wild and cultivated populations of Hevea brasiliensis assessed by nuclear RFLP analysis (1994)
    Springer
    Theoretical and applied genetics 88 (1994), S. 199-207 
    Details
    ISSN: 1432-2242
    Keywords: Hevea brasiliensis ; RFLP ; Nuclear probes ; Isozyme ; Genetic diversity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Restriction fragment length polymorphism was assessed in wild and cultivated populations of Hevea brasiliensis using random probes from an Hevea nuclear library. One-hundred-and-sixty-four individuals were surveyed, and the results discussed in the light of previous work performed on isozyme variation. Both studies show that germplasm collections have led to an effective enrichment of the genetic resources available for Hevea breeding, and that cultivated clones have conserved a relatively high level of polymorphism, despite their narrow genetic base and their high level of inbreeding. An equivalent level of polymorphism is revealed by random nuclear probes and isozymes. However, the genetic structuring of the diversity appears more striking using RFLP markers. Wild accessions can be divided into three genetic groups according to their geographical origin. The present results are an essential guide to the incorporation of wild material in breeding schemes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225898
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  • 8
    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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