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  • Blackwell Publishing Ltd  (6)
  • 2005-2009
  • 2000-2004
  • 1990-1994  (6)
  • 1994  (4)
  • 1990  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Microtubular Systems of Paramecium in Division: Pattern of Cytospindle Assembly (1990)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 37 (1990), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The pattern of cytospindle assembly and the modifications of the microtubular cytoplasmic network during division of Paramecium are studied by means of indirect immunofluorescence. The assembly of cytospindle starts at two independent areas placed respectively around the proter's and opisthe's buccal overture. The moment of the microtubule bundles’appearance depends on their distance from the buccal opening, with those closest appearing 1st. The existence of microtubule organizing centers that act transiently during division of Paramecium is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1990.tb01124.x
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular basis of the optochin-sensitive phenotype of pneumococcus: characterization of the genes encoding the F0 complex of the Streptococcus pneumoniaeStreptococcus oralis H+-ATPases (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 12 (1994), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The gene responsible for the optochin-sensitive (OptS) phenotype of Streptococcus pneumoniae has been characterized. Sequence comparisons indicated that the genes involved encoded the subunits of the F0 complex of an H+-ATPase. Sequence analysis and transformation experiments showed that the atpC gene is responsible for the optochin-sensitive resistant (OptS/OptR) phenotype. Our results also show that natural as well as laboratory OptR isolates have arisen by point mutations that produce different amino acid changes at positions 48, 49 or 50 of the ATPase c subunit. The nucleotide sequence of the F F0 complex of the Streptococcus oralis ATPase has also been determined. In addition, comparison of the sequence of the atpCAB genes of S. pneumoniae R6 (OptS) and M222 (an OptR strain produced by inter-species recombination between pneumococcus and S. oralis), and S. oralis revealed that, in M222, an interchange of atpC and atpA had occurred. We also demonstrate that optochin specifically inhibited the membrane-bound ATPase activity of the S. pneumoniae wild-type (OptS) strains, and found a 100-fold difference between OptS and OptR strains, both in growth inhibition and in membrane ATPase resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1994.tb01045.x
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  • 3
    Electronic Resource
    Electronic Resource
    Involvement of endocytosis in catabolite inactivation of the K+ and glucose transport systems in Saccharomyces cerevisiae (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 121 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The possible relationship between endocytosis and catabolite inactivation of plasma membrane proteins in Saccharomyces cerevisiae has been investigated. Using mutants with an increased rate of endocytosis we have shown that there is a positive correlation between the rate of endocytosis and the rate of inactivation of the K+ and glucose transport systems. It is concluded that endocytosis is involved in catabolite inactivation of these two transport systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07078.x
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of yeast DNA sequences capable of directing transcription in Streptomyces and Escherichia coli (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 115 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Random genomic DNA fragments from Saccharomyces cerevisiae were tested for their ability to activate transcription of a promoterless aminoglycoside phosphotransferase-encoding gene in Streptomyces. About 10% of the insertions led to kanamycin resistance when selected at low concentration (5 μg ml−1). The nucleotide sequences of five insertions that allowed growth at different concentrations of the antibiotic were determined. Three of them contained −10 and −35 consensus sequences for the major class of eubacterial promoters. In two others, a −10 sequence could be identified, but a −35 element was absent at the appropriate distance. All of the five inserts were also transcriptionally active in Escherichia coli and therefore probably belong to the major class of eubacterial promoters. Three of the characterized insertions found to match known yeast sequences did not derive from promoter regions. We conclude that sequences that function as eubacterial promoters occur at random in the yeast genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06625.x
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of ribosomal proteins during growth of Streptomyces coelicolor (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 12 (1994), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Changes in expression of ribosomal protein genes during growth and stationary phase of Streptomyces coelicolor A3(2) in liquid medium were studied. Proteins being synthesized were pulse-labelled with [35 S]-methionine, separated by two-dimensional poly-acrylamide gel electrophoresis, and quantified using the Bioimage computer software. Most of the ribosomal proteins were synthesized throughout the life cycle. Exceptions were two proteins whose synthesis drastically decreased at the approach of stationary phase. These two proteins were identified in purified ribosomes as homologues of Escherichia coli ribosomal proteins L10 and L7/L12, using antibodies raised against fusion proteins between these ribosomal proteins and Escherichia coliβ-galactosldase. The genes (rplJ and rplL) encoding the L10 and L7/L12 proteins were contained in a 1.2 kb BamHl fragment that was cloned and sequenced. The linkage and order of the genes coincide with other L10-L7/L12 operons. However, L11 and L1 genes were not present immediately upstream of the L10 gene, as is the case for E. coli and other bacteria. Instead, two open reading frames of unknown function were found immediately upstream of the L10 gene, in an adjacent 1.9 kb BamHl fragment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1994.tb01027.x
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  • 6
    Electronic Resource
    Electronic Resource
    Biochemical and genetic analysis of an alpha-mannosidase mutant from Saccharomyces cerevisiae (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 69 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A yeast mutant lacking non-specific α-mannosidase activity was found as a background marker during our search for dap2 mutants (Suárez-Rendueles, P. and Wolf, D.H. (1987) J. Bacteriol. 169, 4041–4048). The mutant (DPS-15) is characterized in detail. The mutation called amd1 segregates 2:2 in meiotic tetrads, indicating a single chromosomal gene mutation which is recessive. Diploids heterozygous for amd1 show gene dosage. Thus, it appears that AMD1 might be the structural gene for α-mannosidase. Results obtained with this mutant show that α-mannosidase is not a vital component of the vegetative cell cycle. The differentiation process of sporulation is not disturbed in homozygous mutant diploids. Mannose turnover does not seem to be altered in mutant cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb04192.x
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