Plant Storage Proteins

Shewry, Peter R.

doi:10.1111/j.1469-185x.1995.tb01195.x

Cited by 192 publications

(136 citation statements)

References 294 publications

(196 reference statements)

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“…Combination of multiple structural genes and extensive post-translational processing results in a high degree of polymorphism for these proteins (25). In legume seeds, vicilins exhibit a considerable amount of sequence homology and microheterogeneity and may contribute to plant defense mechanisms (26). The 7S globulins, also known as vicilins, are the major cowpea storage proteins, which are highly heterogeneous and are also encoded by a multigene family (27).…”

Section: Resultsmentioning

confidence: 99%

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Sales

Pimenta²,

Paes

et al. 2001

Braz J Med Biol Res

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The presence of chitin in midgut structures of Callosobruchus maculatus larvae was shown by chemical and immunocytochemical methods. Detection by Western blotting of cowpea (Vigna unguiculata) seed vicilins (7S storage proteins) bound to these structures suggested that C. maculatus-susceptible vicilins presented less staining when compared to C. maculatus-resistant vicilins. Storage proteins present in the microvilli in the larval midgut of the bruchid were recognized by immunolabeling of vicilins in the appropriate sections with immunogold conjugates. These labeling sites coincided with the sites labeled by an anti-chitin antibody. These results, taken together with those previously published showing that the lower rates of hydrolysis of variant vicilins from C. maculatus-resistant seeds by the insects midgut proteinases and those showing that vicilins bind to chitin matrices, may explain the detrimental effects of variant vicilins on the development of C. maculatus larvae.

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Section: Resultsmentioning

confidence: 99%

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Sales

Pimenta²,

Paes

et al. 2001

Braz J Med Biol Res

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“…This conservation is assumed to reflect a crucial role of these cysteine residues in stabilizing the protein structure via disulphide bond formation, but this remains to be established as few components have been disulphide mapped, and no detailed comparisons have been reported. 2S albumin storage proteins have been characterized from a diverse range of plants, including legumes (lupins, peas), crucifers (radish, oilseed rape, Arabidopsis), cotton, sunflower, Brazil nut and castor bean [4]. These are typically heterodimeric proteins, with large and small subunits of Mr about 9000 and 4000, respectively, which arise from post-translational proteolysis of a precursor protein.…”

Section: Introductionmentioning

confidence: 99%

Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily

et al. 1996

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Disulphide mapping of a methionine-rich 2S albumin from sunflower seeds showed four intra-chain disulphide bonds which are homologous with those in a related heterodimeric albumin from lupin seeds (conglutin 5). Similar conserved disulphide bonds are also present in c~-gliadin and T-gliadin storage proteins of wheat, but a lower level of conservation is present in a further related group of proteins, the cereal inhibitors of c~-amylase and trypsin. These differences may relate to the different functions of the proteins.

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“…Most dicotyledonous plant seeds contain 7S and͞or 11S globulins and albumins as the major storage proteins in the embryo or cotyledons, whereas some cereals such as wheat, barley, and corn contain prolamins in the endosperm (1,2). The 11S globulins are distributed more widely than the 7S globulins among plant seeds.…”

mentioning

confidence: 99%

Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer

Adachi

Kanamori

Masuda

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

284

256

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Most plant seeds contain 11S globulins as major storage proteins for their nutrition. Soybean glycinin belongs to the 11S globulin family and consists of five kinds of subunits. We determined the crystal structure of a homohexamer of the glycinin A3B4 subunit at 2.1-Å resolution. The crystal structure shows that the hexamer has 32-point group symmetry formed by face-to-face stacking of two trimers. The interface buries the highly conserved interchain disulfide. Based on the structure, we propose that an ingenious face-to-face mechanism controls the hexamer formation of the 11S globulin by movement of a mobile disordered region to the side of the trimer after posttranslational processing. Electrostatic analysis of the faces suggests that the interchain disulfide-containing face has high positive potential at acidic pH, which induces dissociation of the hexamer into trimers that may be susceptible to proteinases after seed imbibition. This dissociation might result in the degradation and mobilization of 11S globulins as storage proteins in embryos during germination and seedling growth. P lants accumulate protein reserves in developing seeds to act as a sink of nitrogen, sulfur, and carbon. Most dicotyledonous plant seeds contain 7S and͞or 11S globulins and albumins as the major storage proteins in the embryo or cotyledons, whereas some cereals such as wheat, barley, and corn contain prolamins in the endosperm (1, 2). The 11S globulins are distributed more widely than the 7S globulins among plant seeds. Although the quaternary structures of the 7S and 11S globulins are different from each other (the former being a trimeric protein and the latter a hexameric protein), they are believed to be derived from a common ancestor because of the partial homologies in their amino acid sequences and limited proteolysis patterns (3). This assumption has been confirmed by x-ray crystallography of 7S globulins from kidney bean (4), jack bean (5), and soybean (6) and of the trimeric soybean 11S globulin precursor (7).In general, 11S globulins are composed of several kinds of subunits. For example, five major subunits have been identified from soybean: A1aB1b, A2B1a, A1bB2, A3B4, and A5A4B3. In developing seeds, the constituent subunits of 11S globulin are synthesized as a single polypeptide precursor, preproprotein, the signal sequence of which is removed cotranslationally. The resultant proproteins assemble into trimers of Ϸ8S in the endoplasmic reticulum. The proprotein trimers are transported from the endoplasmic reticulum to protein storage vacuoles (PSVs), where they then are cleaved to form acidic and basic polypeptides that are linked by a disulfide bond (8). Finally, the mature proteins assemble into hexamers. The protein reserves are stored in the dormant seed until its germination.Recently we determined the crystal structure of the soybean proglycinin A1aB1b homotrimer at 2.8-Å resolution (7). The protomer consists of N-and C-terminal modules that each include a jelly-roll ␤-barrel and a helix domain. However, the packa...

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Plant Storage Proteins

Cited by 192 publications

References 294 publications

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily

Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer

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