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  • 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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  • 2
    Electronic Resource
    Electronic Resource
    Properties of high-energy pions emitted from heavy-ion collisions at 1 GeV/nucleon (1995)
    Springer
    The European physical journal 352 (1995), S. 175-179 
    Details
    ISSN: 1434-601X
    Keywords: 25.75.+r
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Positively charged pions and protons from collisions of Ne+NaF and Au+Au at 1 GeV/nucleon incident energy were measured near midrapidity. The center-of-mass pion spectra deviate from a Maxwell-Boltzmann distribution. The slope of the high-energy part of the pion spectra varies significantly with the system mass and little with the size of the reaction zone. While the total pion yield rises linearly with the number of participant nucleons, the highenergy component increases more than linearly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01298905
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  • 3
    Electronic Resource
    Electronic Resource
    Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: cDNA, gene structure and developmentally regulated formation (1995)
    Springer
    Plant molecular biology 28 (1995), S. 61-72 
    Details
    ISSN: 1573-5028
    Keywords: biosynthesis ; gene structure ; narbonin ; recombinant protein ; 2S globulin ; seed storage protein ; Victa narbonensis L.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNA and genomic clones encoding narbonin, a 2S globulin from the seed of narbon bean (Vicia narbonensis L.), were obtained using the polymerase chain reaction (PCR) and sequenced. The full-length cDNA as well as genomic clones contain a single open reading frame (ORF) of 873 bp that encodes a protein with 291 amino acids comprising the mature narbonin polypeptide (M r ca. 33 100) and an initiation methionine. The deduced amino acid sequence lacks a transient N-terminal signal peptide. The genomic clones do not contain any intron. No homology was found to nucleic acid and protein sequences so far registered in sequence data libraries. The biosynthesis of narbonin during embryogenesis is developmentally-regulated and its pattern of synthesis closely resembles that of typical seed storage globulins. However, during seed germination narbonin was degraded very slowly, indicating that it may have other function than storage protein. Southern analysis suggests the existence of a small narbonin gene family. Narbonin genes were also found in four different species of the genus Vicia as well as in other legumes such as Canavalia ensiformis and Glycine max. In Escherichia coli a recombinant narbonin was produced which yielded crystals like those prepared from narbonin purified from seeds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042038
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  • 4
    Electronic Resource
    Electronic Resource
    Stable expression of vicilin fromVicia faba with eight additional single methionine residues but failure of accumulation of legumin with an attached peptide segment in tobacco seeds (1995)
    Springer
    Molecular breeding 1 (1995), S. 245-258 
    Details
    ISSN: 1572-9788
    Keywords: legumin ; methionine ; modification ; nutritional value ; Vicia faba ; vicilin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Two different attempts have been undertaken to improve the amino acid composition of storage proteins from field bean (Vicia faba) by genetic engineering. First, legumin was modified to generate a new peptide sequence at the C-terminus containing 4 methionine residues. Second, vicilin was modified by generating 8 single methionine residues distributed over the peptide sequence. The genes were expressed in different systems includingin vitro transcription and translation and stable transformation into tobacco. The modified legumin was found to be unstable when expressed in tobacco seeds. Although specific mRNA was detected on RNA gel blots, no protein could be found by using protein gel blotting and ELISA. Furthermore, a protease preparation able to process the original legumin precursorin vitro degraded the modified legumin precursor. Contrary, the modified vicilin was accumulated in seeds of tobacco transformed with the gene under the control of the seed specific USP promoter. Both the original and the modified vicilin could be detected on protein gel blots at the expected position. Two-dimensional electrophoresis was employed to analyse the expression of original vicilin. Three vicilin-specific products of almost equal size were observed, indicating a slight modification leading to a change of pI. Quantitative determination using competitive ELISA showed that there is no significant difference in accumulation between original and modified vicilin. In both cases, three plants were found with vicilin amounts in the range of 1–3% of total globulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02277425
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  • 5
    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
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