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  • Gene assignment  (1)
  • Vicia faba  (1)
  • Vicia sativa  (1)
  • 1
    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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    Paper (German National Licenses)
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  • 2
    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)
    Fulltext
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