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  • Articles: DFG German National Licenses  (2)
  • Lysine transport  (2)
  • 1
    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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  • 2
    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)
    Fulltext
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