Comparison of Gene Families: Seed Storage and Other Seed Proteins

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.

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Genetic Diversity of Common Bean Genotypes as Revealed By Seed Storage Proteins and Some Agronomic Traits

Plant Breeding and Seed Science ◽

10.2478/v10129-011-0075-1 ◽

2014 ◽

Vol 67 (1) ◽

pp. 125-137 ◽

Cited By ~ 1

Author(s):

Akbar Marzooghian ◽

Mohammad Moghaddam ◽

Mostafa Valizadeh ◽

Mohammad Hasan Kooshki

Keyword(s):

Genetic Diversity ◽

Common Bean ◽

Yield Components ◽

Storage Proteins ◽

Agronomic Traits ◽

Morphological Characteristics ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Seed Morphology

AbstractEvaluation of the genetic diversity present within species is essential for conservation, management and utilization of the genetic resources. The objective of this study was to evaluate genetic variability of 70 common bean genotypes for seed storage proteins, grain morphological characteristics and agronomic traits. Two methods of extracting soluble seed proteins in salt were used.Positive correlations were observed among both seed morphological characters and developmental characters while yield components showed negative correlations with each other. Factor analysis for agronomic and grain morphological traits resulted in three factors were named yield components, seed morphology and phenology, respectively. Most genotypes had lower or medium scores for yield components and phenology factors. Considerable diversity was observed for seed morphology factor among the common bean genotypes.Nei’s diversity coefficient (He= 0.4), effective number of alleles (Ae= 1.69) and number of polymorphic loci (N = 17) indicated larger variation in the extraction method of soluble proteins in low salt (0.2 M NaCl) than high salt (1 M NaCl) condition. Considering that the centers of diversity for common bean are different in seed size, the result of Gst statistics showed that bands with relative mobility of 30, 32, 38 and 40 differentiated two weight groups more than other bands. Furthermore, significant differences were observed between these bands for number of pods per plant and number of seeds per plant.

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The Electrophoretic Contribution to the Solutions of Taxonomical Problems of Some Lathyrus L. Taxa Growing in Turkey

Legume Research - An International Journal ◽

10.18805/lr-569 ◽

2020 ◽

Author(s):

H. Genc ◽

İ. Emre ◽

A. Sahin

Keyword(s):

Seed Storage Protein ◽

Extraction Procedure ◽

Seed Proteins ◽

Seed Storage ◽

Morphological Data ◽

Protein Patterns ◽

Documentation System ◽

Natural Habitats ◽

Protein Assay ◽

Sds Page

Background: The seed proteins are used as molecular markers to clarify the systematic problems. Also, electrophoretic techniques are safe tools to identify the seed proteins. In present study, it was used the SDS-PAGE technique to solve the taxonomical problems of eight taxa of genus Lathyrus belong to three sections Orobus, Lathyrostylis and Pratensis according to the globulin B and glutelin. Methods: The seed materials were collected from natural habitats and 0.5 g seed were homogenized and centrifuged based on extraction procedure. In addition, the amounts of seed storage protein subfractions were determined by using protein assay. The electrophoretic analysis were performed according to the 12% SDS-PAGE. The gel documentation system (Bio-Rad, USA) was used to analyse the electrophoretic data and UPGAMA was used to construct the dendogram to show the relationships among the species under focus. Results: Current study showed that the species of section Pratensis were different from species of sections Orobus and Lathyrostylis. The differences among the studied taxa shown clearly and all studied taxa were choosen from the protein patterns. Furthermore, present study demonstrated that L. nivalis has the highest globulin B and glutelin. Results of the present study generally supported the morphological data.

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Mobilization of seed storage proteins is crucial to high vigor in common bean seeds

Ciência Rural ◽

10.1590/0103-8478cr20200894 ◽

2022 ◽

Vol 52 (2) ◽

Author(s):

Natalia Carolina Moraes Ehrhardt-Brocardo ◽

Cileide Maria Medeiros Coelho

Keyword(s):

Storage Proteins ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Seed Vigor ◽

Intensity Difference ◽

Biochemical Component ◽

Germination Process ◽

Radicle Protrusion ◽

Relationship Of

ABSTRACT: Seed germination is a complex process controlled by many factors, in which physical and biochemical mechanisms are involved and the mobilization of reserves is crucial for this process to occur. Although, seed reserve mobilization is usually thought to be a post-germination process, seed reserve proteins mobilization occurs during germination. This study quantified seed proteins of bean genotypes during different hydration times, in order to understand the process of protein mobilization and whether there is relationship of this biochemical component with seed vigor. This study was conducted using seeds with different levels of vigor, genotypes with highest (13, 42, 55 and 81) and lowest (07, 23, 44, 50, IPR-88-Uirapurú and Iapar 81) physiological quality. High vigor genotypes showed greater efficiency in hydrolysis and mobilization of protein component, because they presented low globulins content in cotyledons at radicle protrusion in relation to low vigor genotypes (07, 23 and 50). The protein alpha-amylase inhibitor, observed in all genotypes, is involved with the longer time needed for radicle protrusion, according to the band intensity difference in genotypes 07, 44 and Iapar 81.

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Identification of prospective sources of agronomically-valuable traits of bread wheat (Triticum aestivum L.) among breeding lines in the condition of Forest-Steppe of Ukraine

Ukrainian Journal of Ecology ◽

10.15421/2020_240 ◽

2020 ◽

Vol 10 (5) ◽

pp. 253-258

Author(s):

S.O. Kovalchuk ◽

S.I. Voloschuk ◽

N.A. Kozub

Keyword(s):

Bread Wheat ◽

Seed Proteins ◽

Seed Storage ◽

Triticum Aestivum L ◽

Wheat Breeding ◽

Brown Rust ◽

Forest Steppe ◽

Breeding Lines ◽

Biochemical Compositions ◽

Moderate Resistance

The aim of work was the estimation of valuable traits of bread wheat breeding lines, obtained from interspecies crosses with wild Aegilops and Triticum species growing in a condition of the Forest-Steppe of Ukraine. We used the seed proteins electrophoresis in PAAG for confirmation of the presence of rye seed storage components in the wheat parental lines genomes. The biochemical compositions of seeds had determined by the infrared spectroscopy method. As a result of researching from the set of 600 breeding lines were selected best lines with increased grain yield from 1 m2, with high protein content in grain, disease resistance, and winter hardiness significantly exceeded the standard variety Polesskaya-90. All lines have high and moderate resistance against diseases: Powdery Mildew, Brown Rust, Septoria Blotch. Based on obtained data had selected breeding lines, which were promising sources of single and complex agronomically valuable traits for bread wheat breeding and genetic researches.

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Polymorphism of buckwheat seed storage proteins in cultivar groups, differing by their morphotype

Agricultural science and practice ◽

10.15407/agrisp6.01.010 ◽

2019 ◽

Vol 6 (1) ◽

pp. 10-17

Author(s):

Ye. Zaika ◽

N. Kozub ◽

I. Sozinov ◽

G. Bidnyk ◽

P. Karazhbey

Keyword(s):

Genetic Markers ◽

Storage Proteins ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Breeding Programs ◽

Cultivar Groups

Aim. To study polymorphism of buckwheat seed proteins in cultivar groups of different morphotypes by the color of corolla. Methods. Electrophoresis by Laemmli method in 17.5 % separating PAAG gel. Results. Electrophoresis spectrum variants with the incidence from 1 to 76 %, common for buckwheat cultivar groups, which are different in their morphotype, were revealed. The obtained results demonstrate a particular level of heterogeneity by the revealed variants in each investigated group of buckwheat genotypes. Variants 2h and 4f, occurring with the incidence of 10 % and 8 % respectively, and specifi c for green-fl owered group of buckwheat cultivars, were also revealed. Conclusions. Different incidence of electrophoresis spectrum components in buckwheat morphotypes, different in fl ower coloring, demonstrates probable different selective value of genes, which control the synthesis of these components or their relation to the genes, closely bound to them. Taking this fact into consideration, buckwheat seed proteins may be molecular and genetic markers for identifi cation of some buckwheat morphotypes, which may be used in breeding programs.

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Engineering sulfur storage in maize seed proteins without apparent yield loss

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1714805114 ◽

2017 ◽

Vol 114 (43) ◽

pp. 11386-11391 ◽

Cited By ~ 25

Author(s):

Jose Planta ◽

Xiaoli Xiang ◽

Thomas Leustek ◽

Joachim Messing

Keyword(s):

Yield Loss ◽

Storage Proteins ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Sulfur Assimilation ◽

Specific Expression ◽

Feeding Trials ◽

The Cost ◽

Reduction Capacity

Sulfur assimilation may limit the pool of methionine and cysteine available for incorporation into zeins, the major seed storage proteins in maize. This hypothesis was tested by producing transgenic maize with deregulated sulfate reduction capacity achieved through leaf-specific expression of the Escherichia coli enzyme 3′-phosphoadenosine-5′-phosphosulfate reductase (EcPAPR) that resulted in higher methionine accumulation in seeds. The transgenic kernels have higher expression of the methionine-rich 10-kDa δ-zein and total protein sulfur without reduction of other zeins. This overall increase in the expression of the S-rich zeins describes a facet of regulation of these proteins under enhanced sulfur assimilation. Transgenic line PE5 accumulates 57.6% more kernel methionine than the high-methionine inbred line B101. In feeding trials with chicks, PE5 maize promotes significant weight gain compared with nontransgenic kernels. Therefore, increased source strength can improve the nutritional value of maize without apparent yield loss and may significantly reduce the cost of feed supplementation.

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Mobilization and synthesis of seed storage and LEA proteins during natural priming of Buddleja cordata and Opuntia tomentosa

Botanical Sciences ◽

10.17129/botsci.1499 ◽

2018 ◽

Vol 96 (1) ◽

pp. 76 ◽

Cited By ~ 1

Author(s):

Sandra Alvarado-López ◽

Ximena Gómez-Maqueo ◽

Diana Soriano ◽

Alma Orozco-Segovia ◽

Alicia Gamboa-de Buen

Keyword(s):

Protein Fraction ◽

Seed Storage Protein ◽

Protein Pattern ◽

Seed Proteins ◽

Seed Storage ◽

Wild Plants ◽

Lea Proteins ◽

Priming Process ◽

Buddleja Cordata ◽

Control Protein

Background: In crop plants, the induction of seed storage protein mobilization and synthesis of LEA family proteins has been extensively described.Question: Natural priming promotes mobilization and synthesis of seed storage and LEA proteins in wild plants?Species studied: Buddleja cordata and Opuntia tomentosa. Study site: Reserva Ecológica del Pedregal de San Angel (REPSA).Methods: Natural priming treatments were applied to B. cordata and O. tomentosa seeds during one and six months respectively. Phosphorylated proteins fractions were obtained by affinity chromatography from control and treated seeds. Differences in protein pattern between control and treated seeds were determined by electrophoresis and the treated seed proteins were identified by LS/LS/MALDITOF. Results: The phosphorylated fraction of B. cordata treated seeds presented two proteins that were absent in the control protein fraction. These two proteins were identified as two different 11S globulins. The phosphorylated fraction of O. tomentosa treated seeds also presented two proteins that were absent in the control protein fraction. These two proteins were identified as a 12S globulin and a LEA protein.Conclusion: Seeds are subjected to changes in soil water content during their permanence in soil; this natural priming process promotes mobilization and synthesis of storage and LEA proteins that are involved in stress resistance.

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Seed proteins mining for development, nutrition and germination using comparative proteomics analysis in quinoa（Chenopodium quinoa willd.)

10.21203/rs.3.rs-19485/v1 ◽

2020 ◽

Author(s):

Suxia Xu ◽

Qingyun Huang ◽

Ziyang Li ◽

Yijin Huang ◽

Chunsong Lin ◽

...

Keyword(s):

Genetic Improvement ◽

Storage Proteins ◽

Chenopodium Quinoa ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Seed Maturation ◽

Purple Acid Phosphatase ◽

Proteomics Analysis ◽

Proteome Changes

Abstract Background Recently quinoa( Chenopodium quinoa willd., 2n=4x=36)raises worldwide popularity with its totally nutrition, stress-tolerance, which leads quinoa to a strategic global food from an Andean native crop. However, seed pre-harvest sprouting, saponin contents e.c., restrict greatly quinoa production and popularity. In the study, we successfully used a combinational proteomics of TMT labeling and parallel reaction monitoring (PRM) to assess proteome changes relating to seed maturation conversion in quinoa to help accelerate genetic improvement for quinoa. Results In total, 6,097 proteins were identified and 4,770 proteins were quantified. Of them, 581 were differential expressed proteins (DEPs). Based on PRM data, seventeen DEPs were identified and quantified, including thirteen down-regulated proteins and four up-regulated proteins. Seventeen DEPs involved in oleanane-type saponins bio-synthesis (β-amyrin 28-oxidase), seed generation (β-Amylase), seed dormancy (late embryogenesis abundant proteins, Cyprosin), seed nutrition (globulin seed storage proteins), accumulation of sugars under seed desiccation (EARLY-RESPONSIVE TO DEHYDRATION 7 protein), pre-harvest sprouting (seed biotin-containing protein SBP65, ABA-inducible protein PHV A1), and enzymes related promoting seed maturation (bifunctional purple acid phosphatase 26), and pigment biosynthesis (3-O-glucosyltransferase). Conclusions We present the high-quality proteomics analysis of quinoa assessing proteome changes during seed maturation conversion. Our results summarize a valuable proteome profiles characterizing quinoa seed maturation. The DEPs are candidate for the functional analyses of proteins regulating seed maturation conversion in quinoa, which provide an important first step towards the genetic improvement of quinoa.

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SDS–PAGE of seed proteins in Festuca (Poaceae): taxonomic implications

Canadian Journal of Botany ◽

10.1139/b91-185 ◽

1991 ◽

Vol 69 (7) ◽

pp. 1425-1432 ◽

Cited By ~ 11

Author(s):

S. G. Aiken ◽

S. E. Gardiner

Keyword(s):

Native Species ◽

Storage Proteins ◽

Polyacrylamide Gel Electrophoresis ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Banding Patterns ◽

Ungerminated Seed ◽

Sds Page ◽

Species Specific

Taxonomically useful descriptors were provided by the banding patterns of seed storage proteins obtained when extracts of bulked, ungerminated seed samples from commercially available North American native species of Festuca were analyzed by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS–PAGE). The banding patterns for three species of rough fescues (section Breviaristatae Krivot) indicate that although the taxa are closely related, F. campestris Rydb. (2n = 56) does not appear to be an autoploid of either F. altaica Trin. (2n = 28) or F. hallii (Vasey) Piper (2n = 28). A distinct band corresponding to a molecular weight of 57 000 occurred in the seed protein profiles of all native and commercial samples of Festuca L. analyzed. The profile for F. californica Vasey, questionably section Breviaristatae, also has a band at this position, and is very different from that of F. altaica, F. campestris, and F. hallii. Species-specific banding patterns were observed for F. brachyphylla Schultes, F. saximontana Rydb., F. idahoensis Elmer, and F. trachyphylla (Hackel) Krajina (F. ovina L. s.l., F. longifolia Thuill., F. ovina var. duriuscula auct. amer.). The results support the recognition of subgenus Schedonorus (Beauv.) Peter., and sections Breviaristatae Krivot and Festuca. Key words: Poaceae, Festuca, SDS–PAGE seed proteins.

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