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  • 1995-1999  (2)
  • Brazil nut protein, grain legumes, leguminB4 promoter  (1)
  • Seed protein genes  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Legumin-like and vicilin-like seed storage proteins: Evidence for a common single-domain ancestral gene (1995)
    Springer
    Journal of molecular evolution 41 (1995), S. 1057-1069 
    Details
    ISSN: 1432-1432
    Keywords: Gene evolution ; Seed protein genes ; Legumin ; Vicilin ; Gene family ; Sequence homology ; Intron/exon structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Legumin-like 11S and vicilin-like 7S globulins are the main storage proteins of most angiosperms and gymnosperms. The subunits of the hexameric legumin are synthesized as a precursor comprising a N-terminal acidic α- and a C-terminal basic β-chain. The trimeric vicilin molecule consists of subunits composed of two symmetrical N- and C-terminal structural domains. In a multiple alignment we have compared the N-terminal and C-terminal domains of 11 legumns and seven vicilins of several dicot, monocot, and gymnosperm species. The comparisons using all six possible pairwise combinations reveal that the N-terminal and C-terminal domains of both protein families are similar to each other. These results together with data on the distribution of variable and conserved regions, on the positions of susceptible sites for proteolytic attack, as well as on the published 7S protein tertiary structure suggest that both protein families share a common single-domain ancestor molecule and lead to the hypothesis that a triplication event has occurred during the evolution of a putative legumin/vicilin ancestor gene. Moreover, the comparison of the intron/exon pattern reveals that at least three out of five intron positions are precisely conserved between the genes of both protein families, further supporting the idea of a common evolutionary origin of recent legumin and vicilin encoding genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00173187
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Seed specific expression of the 2S albumin gene from Brazil nut (Bertholletia excelsa) in transgenicVicia narbonensis (1995)
    Springer
    Molecular breeding 1 (1995), S. 295-301 
    Details
    ISSN: 1572-9788
    Keywords: Brazil nut protein, grain legumes, leguminB4 promoter ; seed storage protein ; sulphur amino acid deficiency ; transgenic plants ; Vicia narbonensis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract In order to evaluate the possibility of enhancing the sulphur amino acids in grain legumes, we have transferred the gene for the methionine-rich 2S albumin from Brazil nut (Bertholletia excelsa) controlled by a seed-specific promoter intoVicia narbonensis. The coding region of the 2S albumin gene that has been completely synthesized was fused to the seed-specific leguminB4 promoter fromVicia faba. Transgenic lines ofV. narbonensis were generated viaAgrobacterium-mediated gene analysis of leaves, stems, roots and seeds of four R0 plants revealed that the expression of the foreign 2S albumin gene occurred in a seed-specific manner and that the foreign protein is present at levels ranging from 1% to 4.8% of total SDS-soluble seed protein. Since the current protocol for transformation ofV. narbonensis has not yet been published, a detailed description of the method is given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02277429
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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