scholarly journals Characterization of Seed Storage Proteins from Chickpea Using 2D Electrophoresis Coupled with Mass Spectrometry

2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
Pramod Kumar Singh ◽  
Nidhi Shrivastava ◽  
Krishna Chaturvedi ◽  
Bechan Sharma ◽  
Sameer S. Bhagyawant
Keyword(s):  
Mass Spectrometry ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Expression Patterns ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Differentially Expressed ◽  
2D Electrophoresis ◽  
Differentially Expressed Proteins ◽  
Amino Acid Homology

Proteomic analysis was employed to map the seed storage protein network in landrace and cultivated chickpea accessions. Protein extracts were separated by two-dimensional gel electrophoresis (2D-GE) across a broad range 3.0–10.0 immobilized pH gradient (IPG) strips. Comparative elucidation of differentially expressed proteins between two diverse geographically originated chickpea accessions was carried out using 2D-GE coupled with mass spectrometry. A total of 600 protein spots were detected in these accessions. In-gel protein expression patterns revealed three protein spots as upregulated and three other as downregulated. Using trypsin in-gel digestion, these differentially expressed proteins were identified by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS) which showed 45% amino acid homology of chickpea seed storage proteins withArabidopsis thaliana.

Revealing genetic diversity in land races and wild accessions of mungbean [Vigna radiata (L.) Wilczek] using SDS-PAGE of seed storage proteins

2015 ◽  
Author(s):  
Ananya Panda ◽  
Swapan K. Tripathy
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Land Races ◽  
Sds Page ◽  
Wild Accessions ◽  
Total Seed

Total seed storage protein profiles of 74 mungbean land races, three wild accessions and a popular variety ‘Jyoti’ of Odisha were analysed by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). 32 genotypes could be clearly identified based on genotype-specific seed protein fingerprints while rest of the test genotypes were categorized into eight protein types. Genotypes included in each protein type had 100% homology and some of these could be duplicates. In this pursuit, a few specific polypeptide markers have been detected for identification of the land races/ genotypes. Dendrogram based on electrophoretic data clustered the genotypes into seven groups at 70% phenon level. Paralakhemundi local, Samarjhola local and Phulbani local-D; and three wild accessions (TCR 20, TCR 213 and TCR 243) were comparatively divergent from other genotypes. Besides, Jyoti, Kalahandi local 2A, Sikri local, kodala local A and TCR 20 were identified to be protein rich with high seed yield. TCR 20 being morphologically similar to mungbean, moderately high protein content and high yielding as well as resistant to drought and bruchids; it may serve as a valuable source genotype in recombination breeding

scholarly journals Phytochemical Evaluation of Moth Bean (Vigna aconitifoliaL.) Seeds and Their Divergence

2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
Neha Gupta ◽  
Nidhi Shrivastava ◽  
Pramod Kumar Singh ◽  
Sameer S. Bhagyawant
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Molecular Weight Range ◽  
Two Dimensional Gel Electrophoresis ◽  
Moth Bean ◽  
Total Seed

In the present study, phytochemical contents of 25 moth bean (Vigna aconitifolia) seed accessions were evaluated. This includes protease inhibitors, phytic acid, radical scavenging activity, and tannins. The studies revealed significant variation in the contents of theses phytochemicals. Presence of photochemical composition was correlated with seed storage proteins like albumin and globulin. Qualitative identification of total seed storage protein abundance across two related moth bean accessions using two-dimensional gel electrophoresis (2D-GE) was performed. Over 20 individual protein fractions were distributed over the gel as a series of spots in two moth bean accessions. Seed proteome accumulated spots of high intensity over a broad range of pI values of 3–10 in a molecular weight range of 11–170 kDa. In both seed accessions maximum protein spots are seen in the pI range of 6–8.

scholarly journals Subunit composition of seed storage proteins in high-protein soybean genotypes

2010 ◽  
Vol 45 (7) ◽  
pp. 721-729 ◽  
Author(s):  
Ksenija Taski-Ajdukovic ◽  
Vuk Djordjevic ◽  
Milos Vidic ◽  
Milka Vujakovic
Keyword(s):  
Protein Content ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
High Protein ◽  
Breeding Programs ◽  
Sds Page ◽  
Soybean Genotypes ◽  
Food Applications

The objective of this work was to quantify the accumulation of the major seed storage protein subunits, β-conglycinin and glycinin, and how they influence yield and protein and oil contents in high-protein soybean genotypes. The relative accumulation of subunits was calculated by scanning SDS-PAGE gels using densitometry. The protein content of the tested genotypes was higher than control cultivar in the same maturity group. Several genotypes with improved protein content and with unchanged yield or oil content were developed as a result of new breeding initiatives. This research confirmed that high-protein cultivars accumulate higher amounts of glycinin and β-conglycinin. Genotypes KO5427, KO5428, and KO5429, which accumulated lower quantities of all subunits of glycinin and β-conglycinin, were the only exceptions. Attention should be given to genotypes KO5314 and KO5317, which accumulated significantly higher amounts of both subunits of glycinin, and to genotypes KO5425, KO5319, KO539 and KO536, which accumulated significantly higher amounts of β-conglycinin subunits. These findings suggest that some of the tested genotypes could be beneficial in different breeding programs aimed at the production of agronomically viable plants, yielding high-protein seed with specific composition of storage proteins for specific food applications.

scholarly journals Nitrogen Supply Drives Senescence-Related Seed Storage Protein Expression in Rapeseed Leaves

Genes ◽  
2019 ◽  
Vol 10 (2) ◽  
pp. 72
Author(s):  
Stefan Bieker ◽  
Lena Riester ◽  
Jasmin Doll ◽  
Jürgen Franzaring ◽  
Andreas Fangmeier ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oilseed Rape ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Nitrogen Deficiency ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nitrogen Supply ◽  
Nutrient Mobilization ◽  
Signaling Molecule

In general, yield and fruit quality strongly rely on efficient nutrient remobilization during plant development and senescence. Transcriptome changes associated with senescence in spring oilseed rape grown under optimal nitrogen supply or mild nitrogen deficiency revealed differences in senescence and nutrient mobilization in old lower canopy leaves and younger higher canopy leaves [1]. Having a closer look at this transcriptome analyses, we identified the major classes of seed storage proteins (SSP) to be expressed in vegetative tissue, namely leaf and stem tissue. Expression of SSPs was not only dependent on the nitrogen supply but transcripts appeared to correlate with intracellular H2O2 contents, which functions as well-known signaling molecule in developmental senescence. The abundance of SSPs in leaf material transiently progressed from the oldest leaves to the youngest. Moreover, stems also exhibited short-term production of SSPs, which hints at an interim storage function. In order to decipher whether hydrogen peroxide also functions as a signaling molecule in nitrogen deficiency-induced senescence, we analyzed hydrogen peroxide contents after complete nitrogen depletion in oilseed rape and Arabidopsis plants. In both cases, hydrogen peroxide contents were lower in nitrogen deficient plants, indicating that at least parts of the developmental senescence program appear to be suppressed under nitrogen deficiency.

Profiling the Seed Storage Protein Among Different Genotypes of Trigonella foenum-graecum L. (Fenugreek)

2019 ◽  
Author(s):  
Nisha . ◽  
Priyanka Khati ◽  
P B Rao
Keyword(s):  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Band ◽  
Trigonella Foenum Graecum ◽  
Trigonella Foenum Graecum L

A qualitative as well as quantitative categorization of seed storage proteins profiles of 23 genotypes of Trigonella foenum- graecum L. were performed by using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) for exploring the level of genetic discrepancy at seed storage protein level. Total soluble proteins were resolved on 10% resolving gel. A dendrogram was constructed on the basis of weight of seed storage proteins, which divide total genotypes into two groups further classified into different sub groups containing different genotypes in them. The bands obtained from gel electrophoresis can serve as a potent tool in discrimination of different genotypes on the basis of their protein content. Proteins with molecular weight 66, 43 and 35 kDa were found in all the genotypes except Fgk-76, PR, Rmt-303, PEB and Rmt-361, The 43 kDa protein band was found missing in Fgk-67, AFg-2, AM-2, AFg-4, Fgk-73, although the protein with 35 kDa weight was present in all the genotypes but not in Rmt-303 same as 63 kDa which is not present in Fgk-70 and 55 kDa protein band was found missing in Fgk-67, Afg-4 and Rmt-361.

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

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.

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 diversity of seed storage proteins in diploid, tetraploid and hexaploid Avena species

2014 ◽  
Vol 60 (2-4) ◽  
pp. 47-54 ◽  
Author(s):  
Honghai Yan ◽  
B. R. Baum ◽  
Pingping Zhou ◽  
Jun Zhao ◽  
Yuming Wei ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Diploid Species ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Tetraploid Species ◽  
Protein Patterns ◽  
Hexaploid Species ◽  
Close Relationship ◽  
Aa Genome

Genetic diversities of 106 Avena accessions, including diploid, tetraploid and hexaploid species, derived from different countries were characterized based on seed storage proteins polymorphism using SDS-PAGE. A total of 24 protein bands and 72 protein patterns were detected in all 106 accessions. The genetic similarity value varied from 0.50 to 1.00. The seed storage protein patterns were largely independent of environmental fluctuation. Accessions of the same species or with identical genome constitutions had the same or similar protein patterns. Relatively lower within-species variations were observed compared with among-species variations. The AACCDD genome hexaploid species and the AA genome diploid species were more divergent than other species, with percentages of polymorphic bands of 85.7% and 61.1% respectively. In the AA genome diploid species, the AsAs genome diploids displayed higher variations than the modified AA genome diploid species. Clustering results showed a close relationship between the hexaploid species and the AACC genome tetraploid species. The AABB genome tetraploid species were similar to the AsAs genome diploid species, with the exception of the species A. agadiriana with AABB genome constitution, which showed a close relationship with the AcAc genome diploid species A. canariensis and the polyploid species carrying the A and C genomes.

scholarly journals Duplication-Dependent CG Suppression of the Seed Storage Protein Genes of Maize

Genetics ◽  
2003 ◽  
Vol 165 (2) ◽  
pp. 835-848
Author(s):  
Gertrud Lund ◽  
Massimiliano Lauria ◽  
Per Guldberg ◽  
Silvio Zaina
Keyword(s):  
Gene Duplication ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Maize Genome ◽  
Ltr Retrotransposons ◽  
Storage Protein Genes ◽  
Zein Genes ◽  
Zein Gene

Abstract This study investigates the prevalence of CG and CNG suppression in single- vs. multicopy DNA regions of the maize genome. The analysis includes the single- and multicopy seed storage proteins (zeins), the miniature inverted-repeat transposable elements (MITEs), and long terminal repeat (LTR) retrotransposons. Zein genes are clustered on specific chromosomal regions, whereas MITEs and LTRs are dispersed in the genome. The multicopy zein genes are CG suppressed and exhibit large variations in CG suppression. The variation observed correlates with the extent of duplication each zein gene has undergone, indicating that gene duplication results in an increased turnover of cytosine residues. Alignment of individual zein genes confirms this observation and demonstrates that CG depletion results primarily from polarized C:T and G:A transition mutations from a less to a more extensively duplicated gene. In addition, transition mutations occur primarily in a CG or CNG context suggesting that CG suppression may result from deamination of methylated cytosine residues. Duplication-dependent CG depletion is likely to occur at other loci as duplicated MITEs and LTR elements, or elements inserted into duplicated gene regions, also exhibit CG depletion.

The role of mRNA and protein sorting in seed storage protein synthesis, transport, and deposition

2005 ◽  
Vol 83 (6) ◽  
pp. 728-737 ◽  
Author(s):  
Andrew J Crofts ◽  
Haruhiko Washida ◽  
Thomas W Okita ◽  
Mio Satoh ◽  
Masahiro Ogawa ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Protein Localization ◽  
Protein Sorting ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Rna Localization ◽  
Endomembrane System

Rice synthesizes and accumulates high levels of 2 distinct classes of seed storage proteins and sorts them to separate intracellular compartments, making it an ideal model system for studying the mechanisms of storage protein synthesis, transport, and deposition. In rice, RNA localization dictates the initial site of storage protein synthesis on specific subdomains of the cortical endoplasmic reticulum (ER), and there is a direct relation between the RNA localization site and the final destination of the encoded protein within the endomembrane system. Current data support the existence of 3 parallel RNA localization pathways leading from the nucleus to the actively synthesizing cortical ER. Additional pathways may exist for the synthesis of cytoplasmic and nuclear-encoded proteins targeted to organelles, the latter located in a stratified arrangement in developing endosperm cells. The study of rice mutants, which accumulate unprocessed glutelin precursors, indicates that these multiple pathways prevent nonproductive interactions between different classes of storage proteins that would otherwise disrupt protein sorting. Indeed, it appears that the prevention of disruptive interactions between different classes of storage proteins plays a key role in their biosynthesis in rice. In addition to highlighting the unique features of the plant endomembrane system and describing the relation between RNA and protein localization, this minireview will attempt to address a number of questions raised by recent studies on these processes.Key words: mRNA localization, protein localization, endomembrane system, seed storage proteins, rice.

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