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  • 1
    Electronic Resource
    Electronic Resource
    A high-affinity iron transport system of Rhizobium meliloti may be required for efficient nitrogen fixation in planta (1991)
    Springer
    Plant and soil 130 (1991), S. 211-217 
    Details
    ISSN: 1573-5036
    Keywords: iron transport ; nitrogen fixation ; nodulation ; Rhizobium ; symbiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract We have analyzed the ability of single site insertion mutants of Rhizobium meliloti 1021 defective in various components of a high-affinity iron transport system to produce nodules, fix nitogen and promote plant growth. Our results indicate that a high-affinity iron transport system may significantly increase the ability of the differentiated form of the bacterium to fix nitrogen and induce an increase in plant growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00011875
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Expression, isolation and properties of Fur (ferric uptake regulation) protein ofEscherichia coli K 12 (1988)
    Springer
    BioMetals 1 (1988), S. 62-68 
    Details
    ISSN: 1572-8773
    Keywords: Fur repressor ; Iron regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The clonedfur (ferric uptake regulation) gene ofEscherichia coli K12 was ligated to an expression vector which was inducible with nalidixic acid. The Fur protein was isolated in a single step by immobilized metal-ion-affinity chromatography over zinc iminodiacetate agarose. The amino acid composition of the isolated protein agreed with that predicted from the gene sequence and indicated post-transcriptional removal of the N-terminal methionine residue. All four cysteines were shown to be present as thiols. Proteolysis with trypsin and chymotrypsin yielded large fragments identifiable on polyacrylamide gel electrophoresis. Various divalent metal ions were found by a nitrocellulose filter binding assay to effect non-specific interaction of the Fur dimer with DNA with a dissociation constant of 7 × 10−12 M. A much smaller value, 2.5 × 10−17 M, was measured by gel mobility retardation assay for binding of Fur to a DNA fragment containing the operator sequences of the aerobactin promoter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01128019
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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