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  • Electronic Resource  (4)
  • Gene assignment  (1)
  • Intron/exon structure  (1)
  • Polymorphism  (1)
  • Sequence homology  (1)
  • Storage protein  (1)
  • Vicia sativa  (1)
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Material
  • Electronic Resource  (4)
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Keywords
  • 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
    Origin and development of protein bodies in cotyledons of Vicia faba (1983)
    Springer
    Planta 157 (1983), S. 401-410 
    Details
    ISSN: 1432-2048
    Keywords: Protein body ; Seed development ; Storage protein ; Vacuole ; Vicia (protein bodies)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397197
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  • 3
    Electronic Resource
    Electronic Resource
    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
    Keywords: cDNA ; Legumin subunits ; Polymorphism ; Gene assignment ; Vicia faba
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00212614
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  • 4
    Electronic Resource
    Electronic Resource
    The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: developmental patterns, intracellular localization and functions in globulin proteolysis (2000)
    Springer
    Plant molecular biology 43 (2000), S. 83-101 
    Details
    ISSN: 1573-5028
    Keywords: cysteine proteinases ; differential gene expression ; enzyme families ; seed globulin proteolysis ; vacuolar localization ; Vicia sativa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Families of papain- and legumain-like cysteine proteinases (CPR) were found in Vicia seeds. cDNAs and antibodies were used to follow organ specificity and the developmental course of CPR-specific mRNAs and polypeptides. Four papain-like cysteine proteinases (CPR1, CPR2, proteinase A and CPR4) from vetch seeds (Vicia sativa L.) were analysed. CPR2 and its mRNA were already found in dry embryonic axes. CPR1 was only detected there during early germination. Both CPR1 and CPR2 strongly increased later during germination. In cotyledons, both CPR1 and CPR2 were only observed one to two days later than in the axis. Proteinase A was not found in axes. In cotyledons it could only be detected several days after seeds had germinated. CPR4 mRNA and polypeptide were already present in embryonic axes and cotyledons during seed maturation and decreased in both organs during germination. Purified CPR1, CPR2 and proteinase A exhibited partially different patterns of globulin degradation products in vitro. Although the cDNA-deduced amino acid sequence of the precursor of proteinase A has an N-terminal signal peptide, the enzyme was not found in vacuoles whereas the other papain-like CPRs showed vacuolar localization. Four different legumain-like cysteine proteinases (VsPB2, proteinase B, VnPB1 and VnPB2) of Vicia species were analysed. Proteinase B and VnPB1 mRNAs were detected in cotyledons and seedling organs after seeds had germinated. Proteinase B degraded globulins isolated from mature vetch seeds in vitro. VsPB2 and proteinase B are localized to protein bodies of maturing seeds and seedlings, respectively, of V. sativa. Like VsPB2 from V. sativa, also VnPB2 of V. narbonensis corresponds to vacuolar processing enzymes (βVPE). Based on these results different functions in molecular maturation and mobilization of storage proteins could be attributed to the various members of the CPR families.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006456615373
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    Paper (German National Licenses)
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