Relationship between the amino acid sequence and the domain structure of the subunits of the 11S seed globulins

Plietz, P.; Drescher, Bernd; Damaschun, G.

doi:10.1016/0141-8130(87)90045-6

Cited by 50 publications

(33 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The pseudoradial-symmetrical structure has been determined for the 11 S globulins from sunflower, rapeseed [lo], faba beans [22] and sesame seed [23]. It was found for other 11 S globulins, too, and represents apparently the common structural type this protein class [20].…”

Section: Fig 1 Lsoelectric Focusing Of the 12 S Globulin From Rapesmentioning

confidence: 99%

“…These two classes of polypeptide chains have been found to exist in the rapeseed globulin, too [ l l , 161. There is, however, a structural peculiarity in the latter which also contains some polypeptide chains linked non-covalently [16,17. The high similarity of the secondary and quaternary structure of the 11 S storage proteins and a certain homology in their primary structure is a proof for the structural relationship between the proteins of this class [14, 18, 191. A general structure model for the 11 S proteins has been derived by PLIETZ et al [20] using published primary structures, secondary structure prediction from these sequence data and the quaternary structure determined by X-ray scattering. Comparing the sequences of both types of polypeptide chains the authors pointed out, that the N-terminal regions of both the a-chains and the P-chains have a conserved sequence which should have a functional or structural meaning.…”

Section: Fig 1 Lsoelectric Focusing Of the 12 S Globulin From Rapesmentioning

confidence: 99%

“…An acidic stretch with a length of 38 residues occurs within the N-terminal region of the cr-chain. Owing to this strongly hydrophilic character, this stretch is assumed to be located at the surface of the molecule like a loop [20].…”

Section: Fig 1 Lsoelectric Focusing Of the 12 S Globulin From Rapesmentioning

confidence: 99%

See 2 more Smart Citations

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

Schwenke

1990

Nahrung

View full text Add to dashboard Cite

Recent data on the structure and chemical modification of the two main storage proteins of rapeseed, the high-molecular mass 12 S globulin and the low-molecular mass 2 S protein (napin) are summarized and compared with those of related seed proteins. The 12 S globulin is built up of six subunits forming a quaternary structure which can be approximated by the model of a trigonal antiprism. The subunits, composed of a larger and a smaller polypeptide chain each, have a two-domain structure which is typical for all related plant proteins. These are characterized by a sedimentation coefficient of 11-13 S, a molecular mass of 300,000-360,000 g/mol and a high percentage of beta-sheet conformation. Increasing succinylation results in a step-by-step dissociation up to the subunits and to an unfolding of the latter at a critical level of modification amounting to 60-70%. These structural changes affect the functional properties remarkably. The napin fraction comprises a group of closely related and highly basic proteins with molecular masses of 12,000-14,000 g/mol, a high content of sulphur-containing amino acids and rich in helical conformation. They are built up of a larger and a smaller disulphide bridged polypeptide chain. Acylation does not abolish the secondary or tertiary structure which are stabilized by inter- and intrachain disulphide bonds. Acylation results, however, in a stabilization of the protein against heat-induced aggregation.

show abstract

Section: Fig 1 Lsoelectric Focusing Of the 12 S Globulin From Rapesmentioning

confidence: 99%

Section: Fig 1 Lsoelectric Focusing Of the 12 S Globulin From Rapesmentioning

confidence: 99%

See 1 more Smart Citation

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

Schwenke

1990

Nahrung

View full text Add to dashboard Cite

show abstract

“…The most studied members of these two groups are the legumins from Pisum sativum, Vicia faba and Glycine max and the vicilins from the same species together with the vicilin-like protein (phaseolin) from Phaseolus vulgaris. Within each group, there is a significant level of sequence similarity between members from different plant species [7,29].…”

Section: Introductionmentioning

confidence: 99%

The sequence of a pea vicilin gene and its expression in transgenic tobacco plants

et al. 1988

View full text Add to dashboard Cite

A 5.5 kb Eco RI fragment containing a vicilin gene was selected from a Pisum sativum genomic library, and the protein-coding region and adjacent 5' and 3' regions were sequenced. A DNA construction comprising this 5.5 kb fragment together with a gene for neomycin phosphotransferase II was stably introduced into tobacco using an Agrobacterium tumefaciens binary vector, and the fidelity of expression of the pea vicilin gene in its new host was studied. The seeds of eight transgenic tobacco plants showed a sixteen-fold range in the level of accumulated pea vicilin. The level of accumulation of vicilin protein and mRNA correlated with the number of integrated copies of the vicilin gene. Pea vicilin was confined to the seeds of transgenic tobacco. Using immunogold labelling, vicilin was detected in protein bodies of eight out of ten embryos (axes plus cotyledons) and, at a much lower level, in two out of eleven endosperms. Pea vicilin was synthesized early in tobacco seed development; some molecules were cleaved as is the case in pea seeds, yielding a major parental component of M r∼50000 together with a range of smaller polypeptides.

show abstract

“…Variability exists within and between species and the environment and genotype contribute D406, page 3 of 11 Dossier D. Chéreau et al: OCL 2016, 23(4) D406 Table 3. Amino acids composition of some albumins and globulins fraction of oilseeds and pulses (Guéguen and Lemarié, 1996;Hughes et al, 2011*) (Plietz et al 1987).…”

Section: Amino Acids Composition Of Albumins and Globulins Fraction Omentioning

confidence: 99%

Combination of existing and alternative technologies to promote oilseeds and pulses proteins in food applications

Chereau¹,

Videcoq²,

Ruffieux³

et al. 2016

OCL

View full text Add to dashboard Cite

-The continuous world population growth induces a total protein demand increase based mainly on plant sources. To meet these global nutritional challenges, existing and innovative dry and wet fractionation processes will have to be combined to better valorise plant protein fraction from pulses and oilseeds. The worldwide success of soy protein isolates originate from the intrinsic qualities of soybean proteins but also from a continuous R&D effort since mid-twenty century. Therefore, the soy protein development model can be applied to protein isolates from diverse pulses and oilseeds meals as rapeseed which has already been recognised as novel food protein in Europe. To boost the delivery of plant proteins, agrofood-industries and academics must pool their respective expertise. Innovative and issue solving R&D projects have to be launched to better valorise pulses and oilseed proteins by (i) creating oil extraction processes which preserve native proteins structure; (ii) developing novel protein extraction processes from lab up to industrial pilot scale; (iii) producing plant protein isolates having comparable foaming, emulsifying or gelling functionality than animal; and (iv) generating hydrolysed proteins with high digestibility adapted to human nutrition. It is also essential to initiate research programs to innovate in wet and dry fractionations of plants or to design in vitro models to evaluate proteins digestibility and allergenicity. The increased awareness regarding plant protein valorisation resulted in the creation by agro-industries and academics of the open platform IMPROVE which propose a combination of competencies and equipment to boost market uptake of Plant Based Proteins.Keywords: Plant / proteins / fractionation / nutrition / functionality Résumé -Combinaison de technologies existantes et alternatives pour promouvoir les protéines d'oléagineux et de légumineuses dans les applications alimentaires. L'augmentation continue de la population mondiale provoque un accroissement de la demande en protéines végétales. Pour répondre au défi, il faudra mieux valoriser la fraction protéique des graines de légumineuses et d'oléo-protéagineux. Le succès des isolats protéiques de soja est dû à leur valeur intrinsèque et à un effort soutenu de recherche depuis les années cinquante. Ce modèle de développement peut s'appliquer aux graines de légumineuses et d'oléo-protéagineux. Déjà, les isolats protéiques de colza ont obtenu le statut Novel Food. Afin d'accélérer la commercialisation de nouvelles fractions protéiques issues de légumineuses et d'oléo-protéagineux, les agroindustriels et les académiques doivent s'associer pour mène des projets R&D innovants visant à (i) créer des procédés d'extraction des lipidiques qui préservent la conformation native des protéines ; (ii) développer de nouveaux procédés d'extraction des protéines de l'échelle laboratoire à l'échelle pilote industrielle ; (iii) produire des isolats protéiques végétaux ayant d'excellentes propriétés fonctionnelles : moussantes, émulsifi...

show abstract

Relationship between the amino acid sequence and the domain structure of the subunits of the 11S seed globulins

Cited by 50 publications

References 24 publications

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

The sequence of a pea vicilin gene and its expression in transgenic tobacco plants

Combination of existing and alternative technologies to promote oilseeds and pulses proteins in food applications

Contact Info

Product

Resources

About