scholarly journals Genetic diversity of the Algerian peanut population analyzed using morphological markers and seed storage proteins

2021 ◽  
Vol 182 (3) ◽  
pp. 111-124
Author(s):  
H. Djeghim ◽  
I. Bellil ◽  
D. Khelifi
Keyword(s):  
Storage Proteins ◽  
Phenotypic Diversity ◽  
Protein Profile ◽  
Principal Component ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
African Countries ◽  
Seed Shape ◽  
Major Interest ◽  
High Level

Background. The peanut is one of the most important oil crops suitable for cultivation in the tropical areas of the world. Despite its agronomic importance, few studies have been carried out to assess the morphogenetic diversity of Arachis hypogaea L., especially in East African countries. The major interest of this morphologic study lies in the potential of this species to provide useful genes for the improvement of cultivated peanuts. To date, no study has been performed in Algeria to characterize local peanut varieties.Materials and methods. Thirty peanut accessions were collected from four principal areas of peanut production in Algeria. Genetic characterization using 15 agronomic characters and 25 morphological descriptors showed a high level of diversity among accessions. Principal Component Analysis and the Hierarchical Ascendant Classification were made to clarify the genetic relationship between peanut accessions.Results and discussion. Results showed that leaflet size (length and width), seed shape and size, oil content, and branching pattern were the principal characters to discriminate the screened A. hypogaea accessions. In addition to that, the weights of 10 pods and 100 seeds were the most variable traits and presented a CV of 42.53% and 40.12%, respectively. On the other hand, total storage proteins extracted were separated using SDS-PAGE and revealed thirty bands that were used to generate a matrix and make a cluster analysis using the UPGMA method, exhibiting different storage proteins compositions. Moreover , the phenotypic diversity observed agrees with the storage protein profile diversity, while the accessions grouped in similar clusters belong to the two subspecies of A. hypogaea. The results of the current study show that morphological traits and seed storage proteins can be useful for exploring the diversity among A. hypogaea accessions.

Taxonomic implications of seed morphology and storage proteins in three tribes of the subfamily Papilionoideae (Fabaceae) in Egypt

Phytotaxa ◽  
2021 ◽  
Vol 484 (1) ◽  
pp. 75-95
Author(s):  
MOSTAFA A. ABOULELA ◽  
ZEINAB A. EL-KAREMY ◽  
HASNAA A. HOSNI ◽  
SARA M. SALEH ◽  
AHMED M. FARIED
Keyword(s):  
Multivariate Analyses ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Morphological Characters ◽  
Seed Morphology ◽  
Seed Shape ◽  
The Core ◽  
Phylogenetic Implications ◽  
And Storage

Papilionoideae is the most species-rich subfamily of Fabaceae. Within Papilionoideae, the “core genistoids” comprise many genera of the tribes Podalyrieae, Thermopsideae, Euchresteae, Crotalarieae, Genisteae, and part of Sophoreae. Seed macro- and micro-morphological characters and seed storage proteins of 12 Egyptian species belonging to three tribes of the core genistoides (Sophoreae, Crotalarieae, and Genisteae) were examined using light microscopy, scanning electron microscopy, and SDS-PAGE electrophoresis. Seed shape, size, surface topography, hilum characteristics, epidermal cell patterns, periclinal cell walls, and anticlinal cell boundaries are described here. Seed protein profiles show variable banding patterns with molecular weights ranging from approximately 5 to 270 kDa. Multivariate analyses based on seed morphology and storage proteins elucidate the phenetic relationships among the investigated species at both the tribal and intrageneric levels. The taxonomic and phylogenetic implications of multivariate analyses are compared with previous and current systematic treatments of the genera within the three tribes. Our results confirm the high taxonomic importance of seed morphology in distinguishing among the investigated species. A key to the species using seed macro- and micro-morphological characters is presented.

scholarly journals Assessment of phenotypic and storage protein diversity in exotic barley cultivated in District Dir (Pakistan)

2019 ◽  
Vol 10 (4) ◽  
pp. 400-405
Author(s):  
M. Ali ◽  
M. Nisar ◽  
W. Khan ◽  
T. Naz ◽  
S. U. Zaman ◽  
...  
Keyword(s):  
Quantitative Traits ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Minimum Variance ◽  
Mean Value ◽  
Variability Index ◽  
Total Seed ◽  
High Level

A total of 198 exotic barley genotypes were collected from the Gene Bank of the Plant Genetic Resource Institute (PGRI), National Agriculture Research Center (NARC), Islamabad, Pakistan, for the assessment of genetic diversity based on morphological and seed storage proteins. Qualitative and quantitative traits were noted as per IPGRI, 1994 descriptor. Among the quantitative parameters, a high level of genetic variability index was noted in seeds per spike at 79.9% of coefficient of variance followed by biomass per plant which shows 37.4% variance, while minimum variance in quantitative traits was noted in days to germination at 5.4% followed by days to maturity at 3.1% with average mean genetic variation in all quantitative traits at 97.6%. Assay of total seed protein in these exotic accessions was analogue through polyacrylamide gel electrophoresis. A high level of variation was noted in loci (bands) B26 (0.98%) followed by B25 (0.89%), B24 (0.78%),B23 (0.69%) and B01 (0.52%). A similarly low level of variation was detected in B03 (0.16%) followed by B06 (0.18%), B13 (0.19%), B12 (0.21%), B11 (0.23%), B05 (0.24%), B07 (0.25%), B21 (0.34%), B20 (0.35%), B17 (0.39%). The results indicate that the mean value of variation in these accessions is 97.6%. Further assessments and exploration were suggested for these genotypes in multi-climatic zones to satisfy farmers’ need, breeders’ interest and malt-industrial requirements.

scholarly journals Assessment of Genetic Diversity in Bambara Groundnut (Vigna subterranea) Landraces Based on Seed Storage Proteins Electrophoretic Pattern

2021 ◽  
Vol 38 (1) ◽  
pp. 40-47
Author(s):  
N.M. Saminu ◽  
B.G. Kurfi ◽  
Y.Y. Muhammad
Keyword(s):  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Protein Profile ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Bambara Groundnut ◽  
Vigna Subterranea ◽  
Research Attention ◽  
Major Cluster

Bambara groundnut (Vigna subterranea) is a leguminous crop that is considered underutilized and has previously received little research attention. Variability in a number of physiological factors, including germination rate, widely affects its production. Seed storage protein, its fractions and protein profile of six Bambara groundnut local landraces were studied to assess their genetic relatedness. Total seed storage protein and its fractions were estimated by Bradford’s method. SDS-PAGE analysis was used to evaluate storage protein profile. The results showed significant differences (p<0.05) in protein contents among the landraces. The major seed storage proteins were found to be globulins (0.048 to 0.088mg/mL ), albumins (0.023 to 0.038mg/mL ), glutelins (0.007 to 0.013mg/mL ) and prolamins (0.002 to 0.004mg/mL ). Five peptide bands were detected with molecular weights corresponding to 97.4 kDa, 45 kDa, 29 kDa, 20.1 kDa and 18 kDa, respectively. Three peptide bands corresponding to 97.4 kDa, 45 kDa and 18 kDa were detected in all the landraces and two peptide bands between 29 kDa and 20.1 kDa were detected in five landraces. Dendrogram generated by UPGMA grouped the six landraces into one major cluster with two sub-clusters. The observed diversity in storage protein pattern of the landraces indicated their potential as materials for crop improvement.

Genetic Effects on the Proportions of Conglutin γ and a Subunit of Conglutin β in the Storage Proteins of Lupinus angustifolius L. Seeds

1981 ◽  
Vol 8 (3) ◽  
pp. 277 ◽  
Author(s):  
RN Oram ◽  
JM Gillespie ◽  
RJ Blagrove
Keyword(s):  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Lupinus Angustifolius ◽  
Β Subunit ◽  
Partial Dominance ◽  
High Level ◽  
Conglutin Γ

The genetic variability in the proportions of conglutin β and γ components of lupin seed storage proteins was explored in F1, F2 and F3 families generated from a cross between two genotypes of Lupinus angustifolius cv. Uniharvest and a white-seeded selection from CPI 47644. The levels of conglutin γ differed by a factor of two in these parents, but varied continuously in the F2 and F3 families, indicating that the parental difference is due to several genes. These parents also differed in the level of a major conglutin β subunit, with a molecular weight of 30 000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the storage globulins from individual F1, F2 and F3 seeds showed that the high level in cv. Uniharvest is controlled by an incompletely dominant allele, Bsc, at one locus, whereas the low level in CPI 47644 (white-seeded) is due to homozygosity for the recessive allele, bsc. The partial dominance of the Uniharvest gene suggests that the locus has a regulatory or processing function, so it has been designated beta subunit controller. F3 families differed significantly in the level of the conglutin β subunit in Bsc/- seeds, indicating that other loci with smaller effects also influence the proportion of this subunit. The proportion of the β subunit in any seed depends largely on its own genotype, and not on the genotype of the maternal plant. The proportion of conglutin γ in the storage proteins varied inversely with the proportion of the β subunit. The implications of these results for the genetic improvement of the biological value of lupin protein are discussed.

The Regulation of Pea Seed Storage Protein Genes by Sulfur Stress

1990 ◽  
Vol 17 (3) ◽  
pp. 355 ◽  
Author(s):  
D Spencer ◽  
WG Rerie ◽  
PJ Randall ◽  
TJV Higgins
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Protein Profile ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Expression Of Genes ◽  
Transfer Procedures ◽  
Storage Protein Genes ◽  
Pea Seed

In this review the role of sulfur in regulating the expression of genes for pea seed storage proteins in both peas and transgenic tobacco is discussed. The levels of the sulfur-containing proteins, legumin and pea albumin 1 (PA1), are reduced in the seeds of peas grown under mild sulfur nutrient stress. In contrast, the levels of sulfur-poor proteins such as pea lectin and vicilin are either unaffected or increased slightly under the same conditions. The levels of all the proteins are a direct reflection of the levels of their respective mRNAs. The reduced levels of legumin and PA1 mRNAs under sulfur stress is known to be due largely to increased mRNA turnover rather than decreased transcription. The advent of gene transfer procedures for plants has allowed re-examination of the mechanism of regulation of mRNA stability under conditions of sulfur stress. A pea albumin 1 gene was engineered for leaf expression and transferred to tobacco and the transgenic plants were grown on normal and low levels of sulfur. Sulfur stress reduces total leaf protein in tobacco by about 20% and there are minor qualitative changes in the total protein profile. In contrast, PA1 levels are reduced by over 90% compared with the controls when the transgenic tobaccos are grown under sulfur stress. Thus, it is clear that sequences responsible for recognising the sulfur status have been included in the transgene. A number of gene constructs have been designed to test where the sulfur-responsive sequences are located in the PA1 gene and some of the preliminary findings are reported.

scholarly journals Wheat (Triticum aestivum L.) TaHMW1D Transcript Variants Are Highly Expressed in Response to Heat Stress and in Grains Located in Distal Part of the Spike

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Temperature Stress ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Filling ◽  
High Temperature Stress ◽  
Two Dimensional Gel Electrophoresis ◽  
Transcript Variants

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.

scholarly journals A Single Seed Protein Extraction Protocol for Characterizing Brassica Seed Storage Proteins

Agronomy ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 107
Author(s):  
Mahmudur Rahman ◽  
Lei Liu ◽  
Bronwyn J. Barkla
Keyword(s):  
Seed Protein ◽  
Storage Proteins ◽  
Protein Extraction ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Yield ◽  
Tissue Type ◽  
Single Seed ◽  
Material Optimization ◽  
Hazardous Chemical

Rapeseed oil-extracted expeller cake mostly contains protein. Various approaches have been used to isolate, detect and measure proteins in rapeseeds, with a particular focus on seed storage proteins (SSPs). To maximize the protein yield and minimize hazardous chemical use, isolation costs and the loss of seed material, optimization of the extraction method is pivotal. For some studies, it is also necessary to minimize or avoid seed-to-seed cross-contamination for phenotyping and single-tissue type analysis to know the exact amount of any bioactive component in a single seed, rather than a mixture of multiple seeds. However, a simple and robust method for single rapeseed seed protein extraction (SRPE) is unavailable. To establish a strategy for optimizing SRPE for downstream gel-based protein analysis, yielding the highest amount of SSPs in the most economical and rapid way, a variety of different approaches were tested, including variations to the seed pulverization steps, changes to the compositions of solvents and reagents and adjustments to the protein recovery steps. Following SRPE, 1D-SDS-PAGE was used to assess the quality and amount of proteins extracted. A standardized SRPE procedure was developed and then tested for yield and reproducibility. The highest protein yield and quality were obtained using a ball grinder with stainless steel beads in Safe-Lock microcentrifuge tubes with methanol as the solvent, providing a highly efficient, economic and effective method. The usefulness of this SRPE was validated by applying the procedure to extract protein from different Brassica oilseeds and for screening an ethyl methane sulfonate (EMS) mutant population of Brassica rapa R-0-18. The outcomes provide useful methodology for identifying and characterizing the SSPs in the SRPE.

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