Gene Families Encoding Isoforms of Two Major Sesame Seed Storage Proteins, 11S Globulin and 2S Albumin†

2006 ◽  
Vol 54 (25) ◽  
pp. 9544-9550 ◽  
Author(s):  
Eric S. L. Hsiao ◽  
Li-Jen Lin ◽  
Feng-Yin Li ◽  
Miki M. C. Wang ◽  
Ming-Yuan Liao ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Sesame Seed ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
2S Albumin ◽  
11S Globulin

Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame†

1999 ◽  
Vol 47 (12) ◽  
pp. 4932-4938 ◽  
Author(s):  
Sorgan S. K. Tai ◽  
Lawrence S. H. Wu ◽  
Emily C. F. Chen ◽  
Jason T. C. Tzen
Keyword(s):  
Molecular Cloning ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin ◽  
11S Globulin

Seed storage proteins in cultivars and subspecies of alfalfa (Medicago sativa L.)

2000 ◽  
Vol 10 (4) ◽  
pp. 423-434 ◽  
Author(s):  
Joan E. Krochko ◽  
J. Derek Bewley
Keyword(s):  
Medicago Sativa ◽  
Storage Protein ◽  
Species Complex ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Patterns ◽  
2S Albumin ◽  
Two Dimensional Gel Electrophoresis ◽  
11S Globulin

AbstractSeed storage proteins were analysed in 27 varieties of alfalfa (Medicago sativaL.); these included five subspecies (glomerata, caerulea, falcata, hemicycla, praefalcata), seven of the nine sources of Medicago germplasm introduced into North America and a sample of additional cultivars. The protein patterns were remarkably consistent for all of these taxa. One-dimensional and two-dimensional gel electrophoresis revealed only minor differences in polypeptide composition within each of the three major classes of storage protein (7S globulin, 11S globulin, 2S albumin). The slight variations that were found provided no information on either parentage or evolutionary relationships amongst these particular taxa. Nonetheless, persistent and reproducible heterogeneity of some minor polypeptides of 11S globulin (medicagin) may be useful under other circumstances for cultivar identification in alfalfa. Both subfamilies (I and II) of the 11S globulin were strongly expressed in all of the cultivars and subspecies examined. It was concluded that this structural divergence within the 11S storage protein family predated the evolution of the M. sativa L. species complex. Most of the variability in storage proteins was quantitative. However, even this variability was reduced when data were standardized with respect to seed dry weights. The consistent similarities in qualitative and quantitative expression of seed storage proteins amongst all of these taxa suggest a high degree of uniformity in both seed physiology and genetics within the alfalfa species complex.

scholarly journals Seed Storage Proteins, 2S Albumin And 11S Globulin, Associated to Severe Allergic Reactions after Flaxseed Intake

2021 ◽  
Vol 32 (5) ◽  
Author(s):  
C Bueno-Díaz ◽  
C Biserni ◽  
L Martín-Pedraza ◽  
M de las Heras ◽  
C Blanco ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Storage Proteins ◽  
Binding Capacity ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Cross Reactivity ◽  
2S Albumin ◽  
11S Globulin ◽  
Flaxseed Extract

Background: Given the increased popularity of flaxseed in meals, several cases of allergy to these seeds have been reported. Little is known about allergens implicated in hypersensitivity reactions to these seeds. The present work aimed to identify the allergens involved in IgE-mediated reactions in five patients with a clinical history of severe systemic symptoms after flaxseed consumption. Methods: Proteins susceptible to be allergens with IgE-binding capacity were purified from flaxseed extract by chromatographic techniques. Their identification was achieved via MALDI-TOF mass spectrometry. Immunoassays were performed using the five allergic patient’s era either by testing them individually or as a pool. Results: Four out of five patients recognized a low-molecular-mass protein (around 13kDa) by immunoblotting of the flaxseed extract, while two patients recognized a protein of approximately 55 kDa. They were identified by mass spectrometry as flaxseed 2S albumin, included into WHO/IUIS allergen nomenclature as Lin u 1,and 11S globulin, respectively. Inhibition assays revealed in vitro IgE-cross-reactivity of Lin u 1 with peanut and cashew nut proteins, while IgE recognition of 11S globulin by patients’ sera was partially inhibited by several plant-derived sources. Conclusions: Seed storage proteins from flaxseed were involved in the development of severe symptoms in five individuals and exhibited cross-reactivity with other allergenic sources. Besides the severity of flaxseed allergy in patients sensitized to 2S albumin, it is the first time that the 11S globulin is identified as a potential allergen. We consider that these data should be taken into account for a more accurate diagnosis of patients.

Molecular cloning, sequencing, and chromosome mapping of a 1A-encoded ω-type prolamin sequence from wheat

Genome ◽  
2002 ◽  
Vol 45 (4) ◽  
pp. 661-669 ◽  
Author(s):  
Ali Masoudi-Nejad ◽  
Shuhei Nasuda ◽  
Akira Kawabe ◽  
Takashi R Endo
Keyword(s):  
Storage Proteins ◽  
Protein Structures ◽  
Seed Storage ◽  
Chromosome Mapping ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
Start Codon ◽  
Pcr Analysis ◽  
Bread Making ◽  
Deletion Lines

Gliadins are the most abundant component of the seed storage proteins in cereals and, in combination with glutenins, are important for the bread-making quality of wheat. They are divided into four subfamilies, the α-, β-, γ-, and ω-gliadins, depending on their electrophoresis pattern, chromosomal location, and DNA and protein structures. Using a PCR-based strategy we isolated and sequenced an ω-gliadin sequence. We also determined the chromosomal subarm location of this sequence using wheat aneuploids and deletion lines. The gene is 1858 bp long and contains a coding sequence 1248 bp in length. Like all other gliadin gene families characterized in cereals, the ω-gliadin gene described here had characteristic features including two repeated sequences 300 bp upstream of the start codon. At the DNA level, the gene had a high degree of similarity to the ω-secalin and C-hordein genes of rye and barley, but exhibited much less homology to the α- and β-gliadin gene families. In terms of the deduced amino acid sequence, this gene has about 80 and 70% similarity to the ω-secalin and C-hordein genes, respectively, and possesses all the features reported for other gliadin gene families. The ω-gliadin gene has about 30 repeats of the core consensus sequences PQQPX and XQQPQQX, twice as many as other gliadin gene families. Southern blotting and PCR analysis with aneuploid and deletion lines for the short arm of chromosome 1A showed that the ω-gliadin was located on the distal 25% of the short arm of chromosome 1A. By comparison of PCR and A-PAGE profiles for deletion stocks, its genomic location must be at a different locus from gli-A1a in 'Chinese Spring'.Key words: glutenin, omega gliadin, storage protein, Triticum aestivum, secalin.

Identification of four major sesame seed allergens by 2D-proteomics and Edman sequencing — Seed storage proteins as common food allergens

2002 ◽  
Vol 109 (1) ◽  
pp. S288-S288 ◽  
Author(s):  
Kirsten Beyer ◽  
Ludmilla Bardina ◽  
Galina Grishina ◽  
Hugh A Sampson
Keyword(s):  
Storage Proteins ◽  
Sesame Seed ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Food Allergens ◽  
Common Food ◽  
Edman Sequencing

Variability in the 11S globulin fraction of seed storage proteins ofHelianthus (Asteraceae)

1994 ◽  
Vol 193 (1-4) ◽  
pp. 69-79 ◽  
Author(s):  
Jacques Raymond ◽  
Brahim Mimouni ◽  
Jean-Louis Azanza
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Globulin Fraction ◽  
11S Globulin

Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: Seed storage proteins as common food allergens

2002 ◽  
Vol 110 (1) ◽  
pp. 154-159 ◽  
Author(s):  
Kirsten Beyer ◽  
Ludmilla Bardina ◽  
Galina Grishina ◽  
Hugh A. Sampson
Keyword(s):  
Storage Proteins ◽  
Sesame Seed ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Food Allergens ◽  
Common Food ◽  
Edman Sequencing

Functionality of the 2S Albumin Seed Storage Proteins from Sunflower (Helianthus annuusL.)

1996 ◽  
Vol 44 (5) ◽  
pp. 1184-1189 ◽  
Author(s):  
Jacques Guéguen ◽  
Yves Popineau ◽  
Irina N. Anisimova ◽  
Roger J. Fido ◽  
Peter R. Shewry ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin

scholarly journals Stable Accumulation of Modified 2S Albumin Seed Storage Proteins with Higher Methionine Contents in Transgenic Plants

1990 ◽  
Vol 94 (3) ◽  
pp. 970-979 ◽  
Author(s):  
Ann De Clercq ◽  
Martine Vandewiele ◽  
Jozef Van Damme ◽  
Philippe Guerche ◽  
Marc Van Montagu ◽  
...  
Keyword(s):  
Transgenic Plants ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin

Evidence that the N-terminal extension of the Vicieae convicilin genes evolved by intragenic duplications and trinucleotide expansions

Genome ◽  
2001 ◽  
Vol 44 (6) ◽  
pp. 1022-1030 ◽  
Author(s):  
L E Sáenz de Miera ◽  
M Pérez de la Vega
Keyword(s):  
Amino Acids ◽  
Lens Culinaris ◽  
Storage Proteins ◽  
Phylogenetic Analyses ◽  
Single Gene ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
Plant Seed ◽  
Vicilin Gene

This study was aimed to identify lentil (Lens culinaris subsp. culinaris) convicilin genes and to carry out a comparative analysis of these genes in the tribe Vicieae. Convicilins differ from vicilins, a related group of plant seed storage proteins, mainly by the presence of an additional sequence of amino acids in the sequence corresponding to the first exon, referred as the N-terminal extension. A single gene for convicilin, a component of legume seed storage proteins, was identified in the cultivated lentil. In this species, the N-terminal extension is formed by a stretch of 126 amino acids of which 59.2% are charged amino acids: 29.6% glutamic acid, 3.2% aspartic acid, 14.4% arginine, 8.8% lysine, and 3.2% histidine. This lentil convicilin sequence is similar to the sequence of convicilins in other species of the tribe Vicieae. However, the size of the N-terminal extension clearly differs among convicilins. Sequence comparison and phylogenetic analyses including convicilin and vicilin of Vicieae species indicated that the differentiation between vicilins and convicilins predated the differentiation of the two vicilin gene families (47- and 50-kDa vicilins), and that the N-terminal extension evolved mainly by a series of duplications of short internal sequences and triplet expansions, the predominant one being GAA.Key words: convicilin, evolution by duplications, Lens culinaris Medik., lentil, legumes, trinucleotide expansion.

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