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  • Allelopathy  (2)
  • Dps protein  (2)
  • Springer  (4)
  • MDPI Publishing
  • 1
    ISSN: 1432-072X
    Keywords: Key words Cyanobacteria ; Nutrient stress ; Stationary phase ; Dps protein ; DNA-protein complex ; Synechococcus sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A stable DNA/protein complex having an apparent molecular mass of approximately 150 kDa was purified from nitrate-limited cultures of the cyanobacterium Synechococcus sp. strain PCC 7942. Amino-terminal peptide sequencing indicated that the polypeptide was structurally similar to the Dps protein of Escherichia coli; Dps is also known as the product of the starvation- and stationary-phase-inducible gene, pexB. The 150-kDa complex dissociated into a 22-kDa protein monomer after boiling in 2% SDS. The 150-kDa complex preparation had approximately a 10% nucleic acid content and upon dissociation released DNA fragments that were sensitive to S1 nuclease digestion. Immunoblot data indicated that the complex accumulates during stationary phase and during nitrogen, sulfur, and phosphorus limitation. DNA-binding assays indicated that the protein nonspecifically binds both linear and supercoiled DNA. Circular dichroism spectroscopy revealed that the Synechococcus sp. Dps-like protein contains extensive regions of alpha-helical secondary structure. We propose that the 150-kDa complex represents a hexameric aggregate of the Dps-like protein complexed with single-stranded DNA and serves to bind a portion of the chromosomal DNA under nutrient-limited conditions.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Nutrient stress ; Stationary phase ; Dps protein ; DNA-protein complex ; Synechococcus sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A stable DNA/protein complex having an apparent molecular mass of approximately 150kDa was purified from nitrate-limited cultures of the cyanobacterium Synechococcus sp. strain PCC 7942. Amino-terminal peptide sequencing indicated that the polypeptide was structurally similar to the Dps protein of Escherichia coli; Dps is also known as the product of the starvation- and stationary-phase-inducible gene, pexB. The 150-kDa complex dissociated into a 22-kDa protein monomer after boiling in 2% SDS. The 150-kDa complex preparation had approximately a 10% nucleic acid content and upon dissociation released DNA fragments that were sensitive to S1 nuclease digestion. Immunoblot data indicated that the complex accumulates during stationary phase and during nitrogen, sulfur, and phosphorus limitation. DNA-binding assays indicated that the protein nonspecifically binds both linear and supercoiled DNA. Circular dichroism spectroscopy revealed that the Synechococcus sp. Dps-like protein contains extensive regions of alpha-helical secondary structure. We propose that the 150-kDa complex represents a hexameric aggregate of the Dps-like protein complexed with single-stranded DNA and serves to bind a portion of the chromosomal DNA under nutrient-limited conditions.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-1561
    Keywords: Allelopathy ; fire ; monoterpenes ; trichomes ; Conradina canescens ; Pinus ; Schizachyrium scoparium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In an investigation of potential chemical activity of fire-sensitive shrubs in Florida's sand pine scrub community, bioassays of foliar washes ofConradina canescens showed significant inhibitory activity on three native grasses that are known to fuel frequent surface fires; inhibition was concentrated seasonally in spring and summer. Application of runoff fromConradina leaves to one of the grasses caused a 50% reduction in growth over a 20-week period. Isolation of the biologically active fractions from the fresh leaves ofC. canescens yielded numerous monoterpenes, a number of which were identified from a GC-MS reference library and/or MS comparison to authentic compounds: 11 from the diethyl ether extract, 11 from steam distillation, and four from the foliar leaf wash. Numerous other monoterpenes present in the extractions were unknown. The terpenoid fraction completely inhibited seed germination of one of the native grasses and of lettuce. Saturated aqueous solutions of nine of the monoterpenes inhibited germination and radicle growth of two native grasses. SEM views of the leaf surfaces ofConradina reveal secretory trichomes that appear to be the source of the monoterpenes as well as the triterpene, ursolic acid. The biological activity ofC. canescens as a fire-sensitive component of the scrub community is reviewed in light of the chemical evidence.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of chemical ecology 16 (1990), S. 1399-1408 
    ISSN: 1573-1561
    Keywords: Allelopathy ; emulsions ; monoterpenes ; Saccharomyces cerevisiae ; yeast ; suspensions ; droplet size ; toxicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The toxic effects of the allelopathic nonsubstituted monoterpenes β-pinene and limonene on yeast,Saccharomyces cerevisiae, were proportional to the size of the monoterpene droplets in suspension. Both the toxic effects and the size of the droplets in suspension were decreased by adding different solvents with the monoterpene as follows: dimethylsulfoxide – dimethylformamide ≫ ethanol 〉 dioxane. Oxygen consumption was inhibited about 80% by 1 mM β-pinene added in dimethylsulfoxide but less than 10% when β-pinene was added in dioxane. Parallel decreases in droplet size and toxic effects of either monoterpene were also induced by hydrating the monoterpene-dimethylformamide or monoterpene-dimethylsulfoxide before addition to yeast. Molecular aggregation may be a mechanism to potentiate the allelopathic properties of monoterpenes when these associate with diverse soil components.
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