scholarly journals Identification and Characterization of the Seed Storage Proteins and Related Genes of Cannabis sativa L.

2021 ◽  
Vol 8 ◽  
Author(s):  
Xin Sun ◽  
Yao Sun ◽  
Yao Li ◽  
Qiong Wu ◽  
Lei Wang
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Storage Protein ◽  
Cannabis Sativa ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Hemp Seed ◽  
Abundant Protein ◽  
Molecular Weights

Hemp (Cannabis sativa L.) seed is emerging as a novel source of plant protein owing to its rich protein content and reasonable nutritional structure. In the current study, the storage proteins of hemp seed were extracted using different methods. The modified Osborne method yielded maximum extraction of the hemp seed storage proteins, while degreasing had little effect on the hemp seed protein (HSP) extraction. Protein identification results revealed that 11S globulin (edestin) was the most abundant protein in hemp seed, and the molecular weights of the two subunits of this protein were ~35 and 20 kDa, respectively. The second most abundant protein was 2S albumin (Cs2S), with a molecular weight of ~14–15 kDa. The least abundant protein was 7S vicilin-like protein (Cs7S), with a molecular weight of ~47 kDa. Subsequently, gene families encoding these three storage protein classes, including three genes for edestin, two for Cs2S, and one for Cs7S, were cloned and then analyzed for amino acid composition and structure. The three edestins were different in their amino acid sequences and calculated molecular weights. The analysis of coding sequences revealed a higher percentage of similarity (62.7%) between Edestin1 and Edestin3, while the similarity decreased significantly to ~57% between Edestin1 and Edestin2, and 58% between Edestin2 and Edestin3. The calculated protein molecular weight was the highest for the protein encoded by Edestin1 and the smallest for the protein encoded by Edestin2. All three edestins were rich in arginine, while Edestin3 had a higher methionine content relative to that in the other two, which proved that Edestin3 had a better nutritional value. Cs2S and Cs7S were different from those reported in previous studies. Therefore, it could be inferred that amino acid composition varies with different hemp cultivars. The current research brought significant theoretical advance in illuminating the understanding of hemp seed storage protein and would have significance for future research on improving the nutritional quality of hemp seed and developing bioactive peptides.

scholarly journals Amino Acid Sequencing and cDNA Cloning of Rice Seed Storage Proteins, the 13kDa Prolamins, Extracted from Type I Protein Bodies.

1999 ◽  
Vol 16 (2) ◽  
pp. 103-113 ◽  
Author(s):  
Norihiro MITSUKAWA ◽  
Ryoichi KONISHI ◽  
Kunitomo KIDZU ◽  
Kozo OHTSUKI ◽  
Takehiro MASUMURA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cdna Cloning ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Bodies ◽  
Type I ◽  
Rice Seed ◽  
Amino Acid Sequencing

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 Studying common wheat material from crosses with Aegilops biuncialis vis. using markers for chromosome 1U

2019 ◽  
Vol 25 ◽  
pp. 55-59
Author(s):  
N. A. Kozub ◽  
I. A. Sozinov ◽  
H. Ya. Bidnyk ◽  
N. A. Demianova ◽  
O. I. Sozinova ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Bread Making ◽  
Wheat Gene ◽  
The Common ◽  
Gli 1

Aim. The aim of the research was to study common wheat material developed from crosses with Aegilops biuncialis Vis. using storage protein loci as markers for chromosome 1U. Methods. SDS and APAG electrophoreses of seed storage proteins were employed to identify alleles at the Glu-1 and Gli-1 loci. The following markers of chromosome 1U of Ae. biuncialis were used: the Glu-U1 locus encoding high-molecular-weight glutenin subunits located on the long arm (1UL) and the gliadin locus Gli-U1 on the short arm (1US). Results. In F6–F7, elimination of chromosome 1U material with a frequency of about 0.222 proceeded. This indicates selection against unbalanced genotypes, which could be tracked using markers for chromosome 1U. In wheat F4–F6 hybrids from crosses with Ae. biuncialis, we revealed a high frequency of formation of genotypes possessing the 1UL arm and lacking 1US. Conclusions. Since the Glu-U1 locus on the arm 1UL encodes high-molecular-weight subunits which directly determine bread-making quality, the developed wheat material is a source of a new allele of this locus introgressed from Ae. biuncialis for enriching the common wheat gene pool. Keywords: Triticum aestivum, Aegilops biuncialis, storage proteins, introgression.

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.

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.

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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