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 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.

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.

Transcriptional regulation of seed storage protein genes in Arabidopsis and cereals

2011 ◽  
Vol 21 (4) ◽  
pp. 247-254 ◽  
Author(s):  
Dong-Mei Xi ◽  
Cheng-Chao Zheng
Keyword(s):  
Transcriptional Regulation ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Current Knowledge ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Regulatory Elements ◽  
Concerted Action ◽  
Seed Albumins ◽  
Storage Protein Genes

AbstractSeed storage proteins (SSPs) are synthesized during development and the expression of their genes is under tight tissue-specific and temporal transcriptional regulation. In this review we summarize the current knowledge concerning the regulatory steps controlling SSP synthesis in Arabidopsis and cereals, which involves the interaction of cis regulatory elements with corresponding trans-acting factors. In some cases, the regulation of SSP genes requires the concerted action of multiple transcription factors (TFs). There is an evolutionary conservation between the prolamins (the main group of SSPs in many cereal grains) and a major group of dicot seed albumins; this relates to both the regulatory elements and the TFs that are functionally exchangeable between the monocot and dicot species.

scholarly journals Biochemical Aspects of a Serine Protease fromCaesalpinia echinataLam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Priscila Praxedes-Garcia ◽  
Ilana Cruz-Silva ◽  
Andrezza Justino Gozzo ◽  
Viviane Abreu Nunes ◽  
Ricardo José Torquato ◽  
...  
Keyword(s):  
Serine Protease ◽  
Storage Proteins ◽  
Gel Filtration ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Optimum Ph ◽  
Caesalpinia Echinata ◽  
Pepstatin A ◽  
Potential Tool

Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds ofCaesalpinia echinataLam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (Km55.7 μM) in an optimum pH of 7.1, and this activity is effectively retained until50∘C. CeSP remained stable in the presence of kosmotropic anions (PO4 3−,SO4 2−, andCH3COO−) or chaotropic cations (K+and Na+). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. The characteristics of the purified enzyme allowed us to classify it as a serine protease. The role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins.

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.

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.

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