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  • 1
    ISSN: 1438-2199
    Keywords: Amino acids ; Potassium channel ; Yeast ; Transcription regulation ; Spasmolytic and hypotensive drugs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Living cells control their electrical responsiveness by regulating the quality and quantity of channels expressed in the plasma membrane. Regulation of transcription of the voltage-gated ion channels is an important part of the molecular basis of cell energization. However, the factors which control the expression of channels are not well understood. We studied the effect on the transcription of the voltage-gated K+ channel in the yeastSchizosaccharomyces pombe of cations, pH, and therapeutic spasmolytic and hypotensive agents with different mechanisms of action, including accumulation of intracellular cAMP. A highly specific 122 bp domain of the K+ channel between S5 and H5 with a 55% homology with Dros shab and mbk3 was amplified by nested PCR from chromosomal DNAS. pombe. Northern blot revealed a 1.8kb transcript. mRNA dot-blot and RNase-protected analysis revealed factors altering the K+ channel transcription.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 215-224 
    ISSN: 0749-503X
    Keywords: glucose transporter gene ; heterologous expression ; substrate accumulation ; transport energization ; Schizosaccharomyces pombe ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Genomic DNA of the Schizosaccharomyces pombe glucose transporter, GHT1, was obtained by complementation of the glucose transport deficient Sz. pombe strain YGS-5. Here we describe the GHT1 gene that encodes a protein of 565 amino acids with a corresponding molecular mass of 62·5 kDa. This eukaryotic glucose transporter contains 12 putative transmembrane segments and is homologous to the HXT multigene family of S. cerevisiae with several amino acid motifs of this sugar transporter family. It is also homologous to other sugar carriers from human, mouse and Escherichia coli. The function of the Ght1 protein as a glucose transporter was proved both by homologous and heterologous expression in the Sz. pombe mutant YGS-5 and in the S. cerevisiae hxt mutant RE700A, respectively. Both transformed yeast strains transported d-glucose with substrate specificity similar to that in Sz. pombe wild-type cells. Moreover, the cells of the two transformed yeast strains accumulated 2-deoxy-d-glucose, a non-metabolizable d-glucose analogue, with an efficiency similar to Sz. pombe wild-type cells. The ability of the S. cerevisiae mutant RE700A to accumulate 2DG in an ΔμH+dependent manner after transformation with GHT1 provides evidence that the Sz. pombe transporter catalyses an energy-dependent uptake of glucose. The sequence of GHT1 was deposited at EMBL, Outstation EBI, Accession Number X91218. ©1997 John Wiley & Sons, Ltd.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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