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

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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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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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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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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Identification of timothy cultivars by SDS-PAGE analysis of seed storage proteins

Canadian Journal of Plant Science ◽

10.4141/cjps92-148 ◽

1992 ◽

Vol 72 (4) ◽

pp. 1215-1222 ◽

Cited By ~ 1

Author(s):

Q. Cai ◽

M. R. Bullen

Keyword(s):

Storage Proteins ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Phleum Pratense ◽

Environmental Stability ◽

Blue Staining ◽

Coomassie Blue Staining ◽

Coomassie Blue ◽

Sds Page

SDS-PAGE analysis of seed proteins was carried out to identify the cultivars in the forage crop, timothy (Phleum pratense L.). Nineteen cultivars of timothy were examined. Among them five were from Europe and fourteen from North America. In total fifty protein bands were detected in mature seed extract by SDS-PAGE followed by Coomassie blue staining. Except for two pairs, all the cultivars were differentiated by SDS-PAGE analysis of seed storage proteins. In the electrophoretic profile, no protein bands were found to be specific either to European or to North American cultivars which is an indication of their genetic similarity. Twelve samples of cultivar Toro harvested from Alberta and Manitoba (Canada), Idaho and Minnesota (USA) were compared and no significant differences were found in their seed protein banding patterns, which suggests environmental stability of timothy seed proteins.Key words: SDS PAGE, timothy cultivar identification, seed storage proteins

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Combined Proteomic and Metabolomic Profiling of the Arabidopsis thaliana vps29 Mutant Reveals Pleiotropic Functions of the Retromer in Seed Development

International Journal of Molecular Sciences ◽

10.3390/ijms20020362 ◽

2019 ◽

Vol 20 (2) ◽

pp. 362 ◽

Cited By ~ 1

Author(s):

Thomas Durand ◽

Gwendal Cueff ◽

Béatrice Godin ◽

Benoît Valot ◽

Gilles Clément ◽

...

Keyword(s):

Arabidopsis Thaliana ◽

Protein Trafficking ◽

Storage Proteins ◽

Protein Sorting ◽

Seed Storage ◽

Seed Storage Proteins ◽

Seed Vigor ◽

Seed Biology ◽

Cargo Proteins ◽

Vacuolar Protein

The retromer is a multiprotein complex conserved from yeast to humans, which is involved in intracellular protein trafficking and protein recycling. Selection of cargo proteins transported by the retromer depends on the core retromer subunit composed of the three vacuolar protein sorting (VPS) proteins, namely VPS26, VPS29, and VPS35. To gain a better knowledge of the importance of the plant retromer in protein sorting, we carried out a comparative proteomic and metabolomic analysis of Arabidopsis thaliana seeds from the wild-type and the null-retromer mutant vps29. Here, we report that the retromer mutant displays major alterations in the maturation of seed storage proteins and synthesis of lipid reserves, which are accompanied by severely impaired seed vigor and longevity. We also show that the lack of retromer components is counterbalanced by an increase in proteins involved in intracellular trafficking, notably members of the Ras-related proteins in brain (RAB) family proteins. Our study suggests that loss of the retromer stimulates energy metabolism, affects many metabolic pathways, including that of cell wall biogenesis, and triggers an osmotic stress response, underlining the importance of retromer function in seed biology.

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Placement of loci for avenins and resistance to Puccinia coronata to a common linkage group in Avena strigosa

Genome ◽

10.1139/g94-128 ◽

1994 ◽

Vol 37 (6) ◽

pp. 900-903 ◽

Cited By ~ 10

Author(s):

P. J. Rayapati ◽

V. A. Portyanko ◽

M. Lee

Keyword(s):

Linkage Group ◽

Storage Proteins ◽

Polyacrylamide Gel Electrophoresis ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Puccinia Coronata ◽

A Genome ◽

Genes Encoding ◽

Group 1 Chromosomes

Alcohol-soluble seed storage proteins of oat (avenins) were extracted from two diploid accessions representing the A genome and separated by high-resolution acid polyacrylamide gel electrophoresis. Polymorphisms were detected for three clearly resolved protein bands. Linkage analysis of 88 F2:3 families mapped the three bands to a single locus. Integration of avenin segregation data with an RFLP linkage map constructed from the same population, mapped the avenin locus to a linkage group containing a locus conferring resistance to nine isolates of Puccinia coronata. Linkage between genes encoding alcohol-soluble seed proteins and genes for resistance to Puccinia species was also observed for the homoeologous group 1 chromosomes of barley (1H), rye (1R), wheat (1A, 1B, 1D), and chromosomes 4 and 10 of maize.Key words: genetics, seed protein, disease resistance.

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Genetic variation in common bean (Phaseolus vulgaris L.) using seed protein markers

Acta Universitatis Sapientiae Agriculture and Environment ◽

10.2478/ausae-2020-0005 ◽

2020 ◽

Vol 12 (1) ◽

pp. 58-69

Author(s):

Henok Ayelign ◽

Eleni Shiferaw ◽

Faris Hailu

Keyword(s):

Common Bean ◽

Storage Protein ◽

Storage Proteins ◽

Seed Storage Protein ◽

Gene Diversity ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Protein Markers ◽

Mesoamerican Gene Pool

AbstractThe genetic diversity of common bean accessions were assessed using seed storage protein markers. At regional level, accessions from the two major growing regions showed the highest level of gene diversity (H = 0.322, I = 0.485, and H = 0.312, I = 0.473), which can be exploited for the future improvement of the crop. Based on phaseolin, the major storage protein in common bean, the majority of the accessions (86%) were grouped under Mesoamerican gene pool. Seed proteins were also used to differentiate various Phaseolus species, indicating the usefulness of seed storage proteins in species identification in this genus.

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Homology of chromosomes of Triticum macha Dek. et Men. and Triticum aestivum L. as shown with the help of genetic markers

Genome ◽

10.1139/g90-114 ◽

1990 ◽

Vol 33 (5) ◽

pp. 755-757 ◽

Cited By ~ 4

Author(s):

E. V. Metakovsky ◽

Z. A. Iakobashvili

Keyword(s):

Triticum Aestivum ◽

Genetic Analysis ◽

Storage Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Triticum Aestivum L ◽

Close Relationship ◽

Homology Relationship ◽

Relationship Of ◽

Triticum Macha

Inheritance of the storage protein (gliadin and glutenin) genes of Triticum macha Dek. et Men. and their allelism to Triticum aestivum L. genes have been studied. A close homology of at least chromosomes 1A and 1B of the two species has been found. Results confirm a very close relationship between T. macha and T. aestivum.Key words: seed storage proteins, genetic analysis, chromosome homology, relationship of Triticum macha Dek. et Men. and Triticum aestivum L.

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