Sequence Analysis and Expression of One Fructose-Bisphosphate Aldolase Gene in Camellia oleifera

2013 ◽  
Vol 1 (1) ◽  
pp. 30-36 ◽  
Author(s):  
Yanling Zeng ◽  
Xiaofeng Tan ◽  
Baoming Wang ◽  
Hongxu Long ◽  
Shuxian Xu ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Camellia Oleifera ◽  
Fructose Bisphosphate ◽  
Fructose Bisphosphate Aldolase ◽  
Aldolase Gene

Duplication of the structural gene for the plastid-specific isozyme of aldolase in Cicer

Genome ◽  
1991 ◽  
Vol 34 (1) ◽  
pp. 151-155 ◽  
Author(s):  
P. M. Gaur ◽  
A. E. Slinkard
Keyword(s):  
Gene Duplication ◽  
Duplicate Genes ◽  
Fructose Bisphosphate ◽  
Cicer Arietinum L ◽  
True Breeding ◽  
Cicer Species ◽  
Fructose Bisphosphate Aldolase ◽  
Wild Cicer Species ◽  
Aldolase Gene ◽  
Ald Gene

Fructose-bisphosphate aldolase (ALD, EC 4.1.2.13) was analysed in Cicer arietinum L. (the cultivated chickpea) and all eight annual wild Cicer species, C. bijugum Rech., C. chorassanicum (Bge.) M. Pop., C. cuneatum Rich., C. echinospermum Davis, C. judaicum Boiss., C. pinnatifidum J. &S., C. reticulatum Lad., and C. yamashitae Kit. Duplicate genes were identified for the plastid-specific isozyme of ALD in C. arietinum and all wild species except C. yamashitae and one accession of C. reticulatum. Gene duplication was indicated by the presence of a true-breeding five-banded zymotype of the tetrameric plastid ALD in these species. Monogenic inheritance was confirmed for the alleles of one of the loci. The occurrence of ALD gene duplication in most of the annual Cicer species suggests that this duplication is of ancient origin. However, this duplication must have occurred after divergence of Cicer from the closely related genera Pisum and Lens because the plastid ALD is controlled monogenically in these latter two genera.Key words: Cicer, isozymes, aldolase, gene duplication.

scholarly journals Epitope-Based Peptide Vaccine Against Fructose-Bisphosphate Aldolase of Madurella mycetomatis Using Immunoinformatics Approaches

2018 ◽  
Vol 12 ◽  
pp. 117793221880970 ◽  
Author(s):  
Arwa A Mohammed ◽  
Ayman MH ALnaby ◽  
Solima M Sabeel ◽  
Fagr M AbdElmarouf ◽  
Amina I Dirar ◽  
...  
Keyword(s):  
B Cell ◽  
Binding Affinity ◽  
Mhc Class Ii ◽  
Bacterial Infections ◽  
Peptide Vaccine ◽  
Fructose Bisphosphate ◽  
Mhc I ◽  
Strong Binding ◽  
Fructose Bisphosphate Aldolase ◽  
Madurella Mycetomatis

Background: Mycetoma is a distinct body tissue destructive and neglected tropical disease. It is endemic in many tropical and subtropical countries. Mycetoma is caused by bacterial infections ( actinomycetoma) such as Streptomyces somaliensis and Nocardiae or true fungi ( eumycetoma) such as Madurella mycetomatis. To date, treatments fail to cure the infection and the available marketed drugs are expensive and toxic upon prolonged usage. Moreover, no vaccine was prepared yet against mycetoma. Aim: The aim of this study is to predict effective epitope-based vaccine against fructose-bisphosphate aldolase enzymes of M. mycetomatis using immunoinformatics approaches. Methods and materials: Fructose-bisphosphate aldolase of M. mycetomatis sequence was retrieved from NCBI. Different prediction tools were used to analyze the nominee’s epitopes in Immune Epitope Database for B-cell, T-cell MHC class II and class I. Then the proposed peptides were docked using Autodock 4.0 software program. Results and conclusions: The proposed and promising peptides KYLQ show a potent binding affinity to B-cell, FEYARKHAF with a very strong binding affinity to MHC I alleles and FFKEHGVPL that shows a very strong binding affinity to MHC II and MHC I alleles. This indicates a strong potential to formulate a new vaccine, especially with the peptide FFKEHGVPL which is likely to be the first proposed epitope-based vaccine against fructose-bisphosphate aldolase of M. mycetomatis. This study recommends an in vivo assessment for the most promising peptides especially FFKEHGVPL.

scholarly journals In Search of Antioxidant Peptides from Porcine Liver Hydrolysates Using Analytical and Peptidomic Approach

Antioxidants ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 27
Author(s):  
María López-Pedrouso ◽  
José M. Lorenzo ◽  
Paula Borrajo ◽  
Daniel Franco
Keyword(s):  
Antioxidant Capacity ◽  
Amino Acid Residues ◽  
Antioxidant Peptides ◽  
Fructose Bisphosphate ◽  
Porcine Liver ◽  
In Vivo Experiments ◽  
Adequate Quality ◽  
Health Promoting ◽  
Fructose Bisphosphate Aldolase

The search for antioxidant peptides as health-promoting agents is of great scientific interest for their biotechnological applications. Thus, the main goal of this study was to identify antioxidant peptides from pork liver using alcalase, bromelain, flavourzyme, and papain enzymes. All liver hydrolysates proved to be of adequate quality regarding the ratio EAA/NEAA, particularly flavourzyme hydrolysates. The peptidomic profiles were significantly different for each enzyme and their characterizations were performed, resulting in forty-four differentially abundant peptides among the four treatments. Porcine liver hydrolysates from alcalase and bromelain are demonstrated to have the most antioxidant capacity. On the other hand, hydrophobic amino acid residues (serine, threonine, histidine and aspartic acid) might be reducing the hydrolysates antioxidant capacity. Seventeen peptides from collagen, albumin, globin domain-containing protein, cytochrome β, fructose-bisphosphate aldolase, dihydropyrimidinase, argininosuccinate synthase, and ATP synthase seem to be antioxidant. Further studies are necessary to isolate these peptides and test them in in vivo experiments.

scholarly journals Proteomic Analysis of Soybean Leaves in a Compatible and an Incompatible Interaction with Phakopsora Pachyrhizi

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Mateus Rodrigues Pereira ◽  
Bianca Castro Gouvêa ◽  
Francismar Corrêa Marcelino-Guimarães ◽  
Humberto Josué de Oliveira Ramos ◽  
Maurilio Alves Moreira ◽  
...  
Keyword(s):  
Control Measure ◽  
Production Costs ◽  
Soybean Rust ◽  
Phakopsora Pachyrhizi ◽  
Fructose Bisphosphate ◽  
Soybean Genotypes ◽  
Fructose Bisphosphate Aldolase ◽  
Soybean Leaves ◽  
Dimensional Electrophoresis ◽  
Carbonic Anhydrase 1

AbstractAsian soybean rust (ASR), which is incited by the fungus Phakopsora pachyrhizi, is considered one of the most aggressive diseases to the soybean culture. There are no commercial cultivars immune to the pathogen and the control measure currently used is the application of fungicides that harms the environment and increases production costs. For a better understanding of the host’s response to the pathogen at the molecular level, two soybean genotypes were analyzed (PI561356, resistant to ASR and Embrapa 48, susceptible) at 72 hours and 192 hours after inoculation with spores of P. pachyrhizi. Leaf protein profiles of the plants were compared by two-dimensional electrophoresis associated with mass spectrometry (MS). Twenty-two protein spots presented different levels when the two treatments were compared (inoculated vs. non-inoculated). From those, twelve proteins were identified by MS analysis. Some of them are involved in metabolic pathways related to plant defense against pathogens, as in the case of carbonic anhydrase, 1-deoxy-D-xylulose- 5-phosphate reductoisomerase, fructose-bisphosphate aldolase and glutamine synthetase. The possible biochemical-physiological meanings of our findings are discussed.

scholarly journals Na2CO3-Responsive Photosynthetic and ROS Scavenging Mechanisms in Chloroplasts of Alkaligrass Revealed by Phosphoproteomics

2019 ◽  
Author(s):  
Jinwei Suo ◽  
Heng Zhang ◽  
Qi Zhao ◽  
Nan Zhang ◽  
Yongxue Zhang ◽  
...  
Keyword(s):  
Quantitative Proteomics ◽  
Energy Homeostasis ◽  
Thermal Dissipation ◽  
Wild Type ◽  
Ros Scavenging ◽  
Fructose Bisphosphate ◽  
Ps Ii ◽  
Ros Homeostasis ◽  
Fructose Bisphosphate Aldolase ◽  
Regulation Of Photosynthesis

Alkali-salinity exerts severe osmotic, ionic and high-pH stresses to plants. To understand the alkali-salinity responsive mechanisms underlying photosynthetic modulation and reactive oxygen species (ROS) homeostasis, physiological and diverse quantitative proteomics analyses of alkaligrass (Puccinellia tenuiflora) under Na2CO3 stress were conducted. In addition, Western blot, real-time PCR, and transgenic techniques were applied to validate the proteomic results and test the functions of the Na2CO3-responsive proteins. A total of 104 and 102 Na2CO3-responsive proteins were identified in leaves and chloroplasts, respectively. In addition, 84 Na2CO3-responsive phosphoproteins were identified, including 56 new phosphorylation sites in 56 phosphoproteins from chloroplasts, which are crucial for the regulation of photosynthesis, ion transport, signal transduction and energy homeostasis. A full-length PtFBA encoding an alkaligrass chloroplastic fructose-bisphosphate aldolase (FBA) was overexpressed in wild-type cells of cyanobacterium Synechocystis sp. Strain PCC 6803, leading to enhanced Na2CO3 tolerance. All these results indicate that thermal dissipation, state transition, cyclic electron transport, photorespiration, repair of photosystem (PS) II, PSI activity, and ROS homeostasis were altered in response to Na2CO3 stress, and they have improved our understanding of the Na2CO3-responsive mechanisms in halophytes.

Novel interaction of selenium-binding protein with glyceraldehyde-3-phosphate dehydrogenase and fructose-bisphosphate aldolase of Arabidopsis thaliana

2006 ◽  
Vol 33 (9) ◽  
pp. 847 ◽  
Author(s):  
Adamantia Agalou ◽  
Herman P. Spaink ◽  
Andreas Roussis
Keyword(s):  
Arabidopsis Thaliana ◽  
Metabolic Regulation ◽  
Binding Protein ◽  
Binding Assays ◽  
Fructose Bisphosphate ◽  
Metabolic Role ◽  
Fructose Bisphosphate Aldolase ◽  
Direct Binding ◽  
High Degree

The metabolic role and regulation of selenium, particularly in plants, is poorly understood. One of the proteins probably involved in the metabolic regulation of this element is the selenium-binding protein (SBP) with homologues present across prokaryotic and eukaryotic species. The high degree of conservation of SBP in different organisms suggests that this protein may play a role in fundamental biological processes. In order to gain insight into the biochemical function of SBP in plants we used the yeast two-hybrid system to identify proteins that potentially interact with an Arabidopsis thaliana (L.) Heynh. homologue. Among the putative binding partners of SBP, a NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and a fructose-bisphosphate aldolase (FBA) were found as reliable positive candidates. The interaction of these proteins with SBP was confirmed by in vitro binding assays. Previous findings in Escherichia coli, demonstrated the direct binding of selenium to both GAPDH and aldolase. Therefore our results reveal the interaction, at least in pairs, of three proteins that are possibly linked to selenium and suggest the existence of a protein network consisting of at least SBP, GAPDH and FBA, triggered by or regulating selenium metabolism in plant cells.

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