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  • Articles: DFG German National Licenses  (2)
  • Root nodules (structural adaptation) Symbiosis (legume-Rhizobium)  (1)
  • nodules  (1)
  • 1
    ISSN: 1432-2048
    Keywords: Bradyrhizobium ; Oxygen pressure and root nodule structure ; Root nodules (structural adaptation) Symbiosis (legume-Rhizobium) ; Vigna Symbol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nodules of cowpea (Vigna unguiculata (L.) Walp. cv. Vita 3:Bradyrhizobium CB 756) from 28-d-old plants cultured for 23 d with their root systems maintained in O2 levels from 1 to 80% (v/v, in N2) in the external gas phase showed a range of structural changes which have been interpreted in relation to an over- or under-supply of O2. A response to the partial pressure of O2 in the gas phase (pO2) was noted with respect to nodule size, lenticel development, the relative distributions of cortical and infected central tissue, the differentiation of cortex, especially the inner cortex, the frequency and size of infected and uninfected interstitial cells, the volume of extracellular spaces both in cortex and infected tissue, and in the frequency of bacteroids. As a consequence of these changes the surface area of inner cortex relative to the nitrogenase-containing units of fixing tissue (infected cells or bacteroids) was increased by as much as 20-fold. Effectiveness of bacteroid functioning increased from 0.10 ± 0.02 · 10-9 μmol acetylene reduced per bacteroid in air-grown nodules to 0.9 ± 0.16 · 10-9 (same units) per bacteroid in those cultured in 1% O2.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: gene expression ; nodules ; phosphoribosyl aminoimidazole synthetase ; purine biosynthesis ; N assimilation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA (VUpur5) encoding phosphoribosyl aminoimidazole (AIR) synthetase, the fifth enzyme of the de novo purine biosynthesis pathway has been isolated from a cowpea nodule cDNA library. It encodes a 388 amino acid protein with a predicted molecular mass of 40.4 kDa. The deduced amino acid sequence has significant homology with AIR synthetase from other organisms. AIR synthetase is present in both mitochondria and plastids of cowpea nodules [7]. A signal sequence encoded by the VUpur5 cDNA has properties associated with plastid transit sequences but there is no consensus cleavage site as would be expected for a plastid targeted protein. Although the signal sequence does not have the structural features of a mitochondrial targeted protein, it has a mitochondrial cleavage site motif (RX/XS) close to the predicted N-terminus of the mature protein. Southern analysis suggests that AIR synthetase is encoded by a single gene raising questions as to how the product of this gene is targeted to the two organelles. VUpur5 is expressed at much higher levels in nodules compared to other cowpea tissues and the gene is active before nitrogen fixation begins. These results suggest that products of nitrogen fixation do not play a role in the initial induction of gene expression. VUpur5 was expressed in Escherichia coli and the recombinant protein used to raise antibodies. These antibodies recognize two forms of AIR synthetase which differ in molecular size. Both forms are present in mitochondria, although the larger protein is more abundant. Only the smaller protein was detected in plastids.
    Type of Medium: Electronic Resource
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