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  • 1
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Gene evolution ; Seed protein genes ; Legumin ; Vicilin ; Gene family ; Sequence homology ; Intron/exon structure
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00173187
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  • 2
    Digitale Medien
    Digitale Medien
    Book reviews (1977)
    Springer
    Theoretical and applied genetics 49 (1977), S. 151-152 
    Details
    ISSN: 1432-2242
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00281713
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  • 3
    Digitale Medien
    Digitale Medien
    Book reviews (1984)
    Springer
    Theoretical and applied genetics 69 (1984), S. 38-38 
    Details
    ISSN: 1432-2242
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00262534
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  • 4
    Digitale Medien
    Digitale Medien
    Origin and development of protein bodies in cotyledons of Vicia faba (1983)
    Springer
    Planta 157 (1983), S. 401-410 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Protein body ; Seed development ; Storage protein ; Vacuole ; Vicia (protein bodies)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Storage proteins of the field bean (Vicia faba L., var. minor, cv. “Fribo”) are synthesized and accumulated in the cotyledons during stage 2 of seed development. Deposition of protein reserves takes place in the protein bodies. The generation of protein bodies was investigated electronmicroscopically using ultra-thin sections as well as the freeze-fracturing technique. During the initial period of storage protein formation, globulins are deposited in large vacuoles which later are transformed to give increasing numbers of small vacuoles with decreasing size. The vacuoles disappear early during the stage of storage protein formation and generate the first protein bodies. During the subsequent period of maximum storage protein formation, which takes place at the rough endoplasmic reticulum (rER), swollen ER strands appear which seem to be entirely filled with protein, and these generate ER-produced protein vacuoles (ERPVAC). The vesicles are transformed in a manner comparable to the vacuoles in the initial period of developmental stage 2 and thus generate the major quantity of protein bodies. Both processes seem to represent only two variants of an uniform mechanism of protein body generation.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00397197
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  • 5
    Digitale Medien
    Digitale Medien
    Polymorphism of legumin subunits from field bean (Vicia faba L. var. minor) and its relation to the corresponding multigene family (1993)
    Springer
    Theoretical and applied genetics 86 (1993), S. 867-874 
    Details
    ISSN: 1432-2242
    Schlagwort(e): cDNA ; Legumin subunits ; Polymorphism ; Gene assignment ; Vicia faba
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Legumin, which amounts to approximately 55% of the seed protein in field beans (Vicia faba L. var. minor), is a representative of the 12S storage globulin family. The 12S storage globulins are hexameric holoprotein molecules composed of different types of polymorphic subunits encoded by a multigene family. ‘Type-A’ legumin subunits contain methionine whereas ‘type-B’ are methionine-free subunits. Sequencing of two different type A-specific cDNAs, as well as an FPLC/HPLC-based improvement of subunit fractionation and peptide mapping with subsequent partial amino-acid sequencing, permit the assignment of some of the polymorphic legumin subunits to members of the multigene family. Two different type A subunits (A1 and A2) correspond to the two different cDNA clones pVfLa129 (A2) and 165 (A1), but microheterogeneity in the amino-acid sequences indicates that polymorphic variants of both representatives of this type may exist. Two groups of published type B-specific gene sequences (LeB7, and LeB2, LeB4, LeB6, respectively) are represented by two polymorphic subunit fractions (B3I, B3II, and B4I, B4II). A seventh clone, LeB3, encodes one of the large legumin subunits that is only a minor component of the legumin seed protein complex.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00212614
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  • 6
    Digitale Medien
    Digitale Medien
    Book reviews (1970)
    Springer
    Theoretical and applied genetics 40 (1970), S. 286-288 
    Details
    ISSN: 1432-2242
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00282039
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  • 7
    Digitale Medien
    Digitale Medien
    Book reviews (1977)
    Springer
    Theoretical and applied genetics 51 (1977), S. 143-144 
    Details
    ISSN: 1432-2242
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00273827
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  • 8
    Digitale Medien
    Digitale Medien
    Book reviews (1978)
    Springer
    Theoretical and applied genetics 53 (1978), S. 283-284 
    Details
    ISSN: 1432-2242
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00280992
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  • 9
    Digitale Medien
    Digitale Medien
    Book reviews (1978)
    Springer
    Theoretical and applied genetics 53 (1978), S. 191-192 
    Details
    ISSN: 1432-2242
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00273579
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  • 10
    Digitale Medien
    Digitale Medien
    The sulphur-rich Brazil nut 2S albumin is specifically formed in transgenic seeds of the grain legume Vicia narbonensis (1955)
    Springer
    Euphytica 85 (1955), S. 181-192 
    Details
    ISSN: 1573-5060
    Schlagwort(e): Vicia narbonensis ; gene transfer ; gene expression ; seeds ; 2S albumin ; methionine
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft
    Notizen: Summary Epicotyl explants were co-cultivated with Agrobacterium tumefaciens EHA101 to transfer a chimeric 2S albumin gene construct carried in the binary Ti plasmid vectors pGSGLUC1 or pGA472 into the grain legume Vicia narbonensis. This gene encoding the sulphur-rich Brazil nut albumin was under the control of either the CaMV 35S promoter which permits gene expression in all organs, or the Vicia faba legumin B4 promoter which elicits seed-specific gene expression. After callus formation and selection for kanamycin resistance, somatic embryos were induced which, in the case of transformation with the vector pGSGLUC1, were screened for GUS activity. Embryos that produced GUS were in addition analysed for 2S albumin formation. Selected transgenic embryos were cloned by multiple shoot regeneration. Rooted and fertile plants were obtained by grafting transgenic shoots on the appropriate seedlings. R1 and R2 generations were raised and analysed for GUS as well as 2S albumin gene expression. Expression of the 35S promoter/2S albumin gene fusion took place in all organs of the transgenic plants including the cotyledons of seeds, whereas seed-specific gene expression was found in transformants with the legumin promoter/2S albumin gene fusion. The 2S albumin accumulated in the 2S protein fraction of transgenic seeds and its primary translation product was processed into the 9 and 3 kDa polypeptide chains. The foreign protein was localised in the protein bodies of the grain legume. Analysis of the R2 plants indicated Mendelian inheritance of the 2S albumin gene. In homozygous V. narbonensis plants the amounts of 2S albumin were twice that present in the corresponding heterozygous plants. Whereas only low level formation of the foreign protein was achieved if the gene was under the control of the 35S promoter, approximately 3.0% of the soluble seed protein was 2S albumin if seed-specific gene expression was directed by the legumin B4 promoter. Some of these transformants exhibited a three-fold increase in the methionine content of the salt-soluble protein fraction extracted from seeds.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00023947
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