scholarly journals Mobilization and synthesis of seed storage and LEA proteins during natural priming of Buddleja cordata and Opuntia tomentosa

2018 ◽  
Vol 96 (1) ◽  
pp. 76 ◽  
Author(s):  
Sandra Alvarado-López ◽  
Ximena Gómez-Maqueo ◽  
Diana Soriano ◽  
Alma Orozco-Segovia ◽  
Alicia Gamboa-de Buen
Keyword(s):  
Protein Fraction ◽  
Seed Storage Protein ◽  
Protein Pattern ◽  
Seed Proteins ◽  
Seed Storage ◽  
Wild Plants ◽  
Lea Proteins ◽  
Priming Process ◽  
Buddleja Cordata ◽  
Control Protein

<p><strong>Background</strong><strong>:</strong> In crop plants, the induction of seed storage protein mobilization and synthesis of LEA family proteins has been extensively described.</p><p><strong>Question</strong><strong>:</strong> Natural priming promotes mobilization and synthesis of seed storage and LEA proteins in wild plants?</p><p><strong>Species</strong> <strong>studied</strong><strong>:</strong> <em>Buddleja cordata </em>and<em> Opuntia tomentosa. </em></p><p><strong>Study</strong> <strong>site</strong><strong>:</strong> Reserva Ecológica del Pedregal de San Angel (REPSA).</p><p><strong>Methods</strong><strong>:</strong> Natural priming treatments were applied to <em>B. cordata</em> and <em>O. tomentosa </em>seeds during one and six months respectively. Phosphorylated proteins fractions were obtained by affinity chromatography from control and treated seeds. Differences in protein pattern between control and treated seeds were determined by electrophoresis and the treated seed proteins were identified by LS/LS/MALDITOF. </p><p><strong>Results</strong><strong>:</strong> The phosphorylated fraction of <em>B. cordata</em> treated seeds presented two proteins that were absent in the control protein fraction. These two proteins were identified as two different 11S globulins.  The phosphorylated fraction of <em>O. tomentosa</em> treated seeds also presented two proteins that were absent in the control protein fraction. These two proteins were identified as a 12S globulin and a LEA protein.</p><p><strong>Conclusion</strong><strong>:</strong> Seeds are subjected to changes in soil water content during their permanence in soil; this natural priming process promotes mobilization and synthesis of storage and LEA proteins that are involved in stress resistance. </p>

The Electrophoretic Contribution to the Solutions of Taxonomical Problems of Some Lathyrus L. Taxa Growing in Turkey

2020 ◽  
Author(s):  
H. Genc ◽  
İ. Emre ◽  
A. Sahin
Keyword(s):  
Seed Storage Protein ◽  
Extraction Procedure ◽  
Seed Proteins ◽  
Seed Storage ◽  
Morphological Data ◽  
Protein Patterns ◽  
Documentation System ◽  
Natural Habitats ◽  
Protein Assay ◽  
Sds Page

Background: The seed proteins are used as molecular markers to clarify the systematic problems. Also, electrophoretic techniques are safe tools to identify the seed proteins. In present study, it was used the SDS-PAGE technique to solve the taxonomical problems of eight taxa of genus Lathyrus belong to three sections Orobus, Lathyrostylis and Pratensis according to the globulin B and glutelin. Methods: The seed materials were collected from natural habitats and 0.5 g seed were homogenized and centrifuged based on extraction procedure. In addition, the amounts of seed storage protein subfractions were determined by using protein assay. The electrophoretic analysis were performed according to the 12% SDS-PAGE. The gel documentation system (Bio-Rad, USA) was used to analyse the electrophoretic data and UPGAMA was used to construct the dendogram to show the relationships among the species under focus. Results: Current study showed that the species of section Pratensis were different from species of sections Orobus and Lathyrostylis. The differences among the studied taxa shown clearly and all studied taxa were choosen from the protein patterns. Furthermore, present study demonstrated that L. nivalis has the highest globulin B and glutelin. Results of the present study generally supported the morphological data.

scholarly journals Suitability of oat-seed storage-protein markers for identification of cultivars in grain and mixed flour samples

2011 ◽  
Vol 49 (No. 11) ◽  
pp. 486-491 ◽  
Author(s):  
V. Dvořáček ◽  
V. Čurn ◽  
J. Moudrý
Keyword(s):  
Protein Fraction ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Protein Markers ◽  
Protein Patterns ◽  
Identification Procedure ◽  
Naked Oat ◽  
Sds Page ◽  
Oat Cultivars ◽  
Naked Oats

The objective of this study was an improvement on oat identification procedure for laboratory applications, and the comparison of albumin-globulin and avenin protein patterns in five hulled and naked oat cultivars: Abel (CZ) and Iz&aacute;k (CZ) &ndash; naked oats, Auron (CZ), Edmund (D) and Expander (D) &ndash; hulled oats. The last object of this study was the authenticity verification of standardly prepared meal samples with various proportions of admixture. It was confirmed that avenins, characterised under SDS-PAGE conditions, are reliable implements for the identification of oat cultivars. It was found that oat grain contains, on the basis of Osborne fractionation, another significant protein fraction &ndash; glutelins. The question of the protein fraction analysis that was used for the admixture identification stays still open. In sufficiently different cultivars, the certainty of the admixture detection in meal samples may be high. Nevertheless, in other cases (higher cultivar similarity) it will be necessary to use some other, more sensitive techniques.

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 A Proteomic Analysis of Seed Proteins Expressed in a Brassica Somatic Hybrid and its two Parental Species

2014 ◽  
Vol 24 (1) ◽  
pp. 11-26 ◽  
Author(s):  
M. M. Hossain ◽  
X. Li ◽  
I. H. Evans ◽  
M.A. Rahman
Keyword(s):  
Chinese Cabbage ◽  
Somatic Hybrid ◽  
Seed Storage Protein ◽  
Seed Proteins ◽  
Seed Storage ◽  
Late Embryogenesis Abundant ◽  
Hybrid Vigour ◽  
Vegetable Crops ◽  
2D Gel ◽  
The Tropics

Cabbage (Brassica oleracea) is one of the world’s major vegetable crops. However, the cabbage plant cannot be readily vernalized and produce seed in the tropics, whereas Chinese cabbage (Brassica campestris) can be conveniently vernalized at the seed stage. Proteins from seeds of an IPSA cabbage-Chinese cabbage somatic hybrid showing both hybrid vigour and the seed-stage vernalization characteristic were analyzed and compared with those of its two parents.  1D gel analysis indicated some differential expression of the seed proteins. Furthermore,  in 2D, gel analysis, 13 differentially expressed protein spots were examined:  of these ten were found to belong to the cruciferin seed storage protein complex, two were unidentifiable (no MASCOT match), and one was identified as late embryogenesis Abundant (LEA)-like protein, and was present only in the cabbage parent. This LEA-like protein in cabbage seed could therefore be implicated in interfering with the vernalization process in the tropics. Plant Tissue Cult. & Biotech. 24(1): 11-26, 2014 (June) D. O. I. http://dx.doi.org/10.3329/ptcb.v24i1.19187

scholarly journals Seed storage protein electrophoretic profile among popular cultivars of date palm (Phoenix dactylifera L.)

2020 ◽  
Vol 49 (4) ◽  
pp. 1063-1069
Author(s):  
Sadia Abdul Hayee ◽  
Sabeena Rizwan ◽  
Ashif Sajjad ◽  
Uzma Jabeen ◽  
Farrukh Bashir ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Molecular Weight ◽  
Storage Protein ◽  
Date Palm ◽  
Seed Storage Protein ◽  
Seed Proteins ◽  
Seed Storage ◽  
Phoenix Dactylifera ◽  
Molecular Weight Range ◽  
Electrophoretic Profile

Evaluation of the seed storage protein electrophoretic profile among popular cultivars of date palm (Pheonix dactylifera) available in different regions of Balochistan, Pakistan was conducted. The genetic diversity of seed proteins of 12 cultivars were examined by electrophoresis. Twenty one protein bands with different mobility rates were identified within a molecular weight range of 11 to 351 KDa. The cultivar from Panjgur (Soorri) was well resolved on SDS-PAGE from the all other cultivars and gave the highest number of intense bands due to unique genetic build up. Genetic diversity among cultivars was evaluated by constructing the dendrogram for protein bands, which showed the cultivar (SP1) which is significantly different from all other cultivars on the basis of similarities in molecular weight of proteins.

scholarly journals Molecular cytogenetical and biochemical studies on some Lupinus species

2021 ◽  
Vol 45 (1) ◽  
Author(s):  
Hoda B. M. Ali ◽  
Samy A. A. Heiba
Keyword(s):  
Related Species ◽  
Storage Protein ◽  
Seed Storage Protein ◽  
Lupinus Albus ◽  
Seed Storage ◽  
Rrna Genes ◽  
Large Chromosome ◽  
45S Rdna ◽  
Lupinus Polyphyllus ◽  
Electrophoretic Patterns

Abstract Background Lupins are cultivated as human consumption grains and forage legumes. The chromosomes of lupins are too small to be karyotyped by conventional techniques, because they reveal a general lack of distinctive cytological features. In the current study, Fluorescence in situ Hybridization (FISH) was used to locate 5S and 45S ribosomal gene sites on the chromosomes of Lupinus albus ssp albus, Lupinus albus ssp graecus, Lupnus termis (all with 2n = 50), and Lupinus polyphyllus lindl var. polyphyllus (2n = 48), FISH together with seed storage protein electrophoretic patterns were used to find out the relationship among these species. Results The double-target FISH on the chromosomes of the studied species with rDNA probes revealed that the two types of rRNA genes are located on different chromosomes. The detected loci of rRNA genes partially reflected the taxonomical similarity among the two Lupinus albus subspecies and L. termis. Lupinus polyphyllus lindl var. polyphyllus was exception by having unique large chromosome mostly is covered by one signal of 45S rDNA, whereas its homologous chromosome seems to be normal-sized and have the other 45S rDNA locus. The similarity matrix among the Lupinus species as computed according to Jaccardʼs Coefficient from the SDS-PAGE, showed that L. albus ssp. Albus and L. albus ssp. Graecus are the most similar species (~ 97%), and then comes L. termis, and L. polyphyllus lindl var. polyphylus has been placed in separate clade and still the most related species to it among the studied species is L. termis (~ 70%). Conclusion It could be postulated from FISH and seed storage protein electrophoretic patterns that the relationships among the studied species is as follows, Lupinus albus ssp albus, is the most related species to Lupinus albus ssp graecus then comes Lupnus termis and Lupinus polyphyllus lindl var. polyphyllus at a distal position.

Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family

2002 ◽  
Vol 110 (1) ◽  
pp. 160-166 ◽  
Author(s):  
Fang Wang ◽  
Jason M. Robotham ◽  
Suzanne S. Teuber ◽  
Pallavi Tawde ◽  
Shridhar K. Sathe ◽  
...  
Keyword(s):  
Storage Protein ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Protein Family
Sign in / Sign up

Export Citation Format

Share Document