scholarly journals MATE-Type Proteins Are Responsible for Isoflavone Transportation and Accumulation in Soybean Seeds

2021 ◽  
Vol 22 (21) ◽  
pp. 12017
Author(s):  
Ming-Sin Ng ◽  
Yee-Shan Ku ◽  
Wai-Shing Yung ◽  
Sau-Shan Cheng ◽  
Chun-Kuen Man ◽  
...  
Keyword(s):  
Animal Feed ◽  
Cell Model ◽  
Vacuolar Membrane ◽  
Food Crops ◽  
Soybean Seeds ◽  
Transgenic Soybean ◽  
Bona Fide ◽  
Isoflavone Biosynthesis ◽  
Seed Isoflavone ◽  
Total Seed

Soybeans are nutritionally important as human food and animal feed. Apart from the macronutrients such as proteins and oils, soybeans are also high in health-beneficial secondary metabolites and are uniquely enriched in isoflavones among food crops. Isoflavone biosynthesis has been relatively well characterized, but the mechanism of their transportation in soybean cells is largely unknown. Using the yeast model, we showed that GmMATE1 and GmMATE2 promoted the accumulation of isoflavones, mainly in the aglycone forms. Using the tobacco BrightYellow-2 (BY-2) cell model, GmMATE1 and GmMATE2 were found to be localized in the vacuolar membrane. Such subcellular localization supports the notion that GmMATE1 and GmMATE2 function by compartmentalizing isoflavones in the vacuole. Expression analyses showed that GmMATE1 was mainly expressed in the developing soybean pod. Soybean mutants defective in GmMATE1 had significantly reduced total seed isoflavone contents, whereas the overexpression of GmMATE1 in transgenic soybean promoted the accumulation of seed isoflavones. Our results showed that GmMATE1, and possibly also GmMATE2, are bona fide isoflavone transporters that promote the accumulation of isoflavones in soybean seeds.

Antisense RNA-mediated GmFAD2-1B Gene Silencing Enhances Accumulation of Oleic Acid in Transgenic Soybean Seeds

2017 ◽  
Vol 43 (11) ◽  
pp. 1588 ◽  
Author(s):  
Jing YANG ◽  
Guo-Jie XING ◽  
Lu NIU ◽  
Hong-Li HE ◽  
Qian DU ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Gene Silencing ◽  
Antisense Rna ◽  
Soybean Seeds ◽  
Transgenic Soybean

Fumonisin Production in Corn by Toxigenic Strains of Fusarium moniliforme and Fusarium proliferatum

1994 ◽  
Vol 57 (6) ◽  
pp. 514-521 ◽  
Author(s):  
CHARLES W. BACON ◽  
PAUL E. NELSON
Keyword(s):  
Fusarium Moniliforme ◽  
Fruits And Vegetables ◽  
Animal Feed ◽  
Fusaric Acid ◽  
Fumonisin B1 ◽  
Fusarium Proliferatum ◽  
Food Crops ◽  
Ear Rot ◽  
Corn Products ◽  
Toxigenic Strains

The fungi Fusarium moniliforme Sheldon and Fusarium proliferatum (Matsushima) Nirenberg produce a series of toxins on corn which include the fumonisins of which fumonisin B1 and B2 are considered to have cancer promoting activity. Both fungi produce similar ratios of the fumonisins B1 to B2. Other mycotoxins produced include moniliformin, fusarin C and fusaric acid. Fumonisin B1 has been shown to be responsible for most of the toxicological affects observed from ingesting corn infected by toxigenic isolates of these fungi. The distribution of the two fungi is generally similar, although F. proliferatum is isolated more frequently from sorghum than corn. They occur worldwide on other food crops, such as rice, sorghum, millet, several fruits and vegetables. Both fungi are ear rot pathogens of corn, thus, mycotoxin production occurs under field conditions, although it also may occur in storage. One or both fungi may have a frequency of occurrence of 90% or higher in corn; 90% of the F. moniliforme isolates produce the fumonisins. On corn and corn products the range of concentrations reported is 0.3 to 330 μg/g of corn-based product. These concentrations include both corn-based animal feed and human foods.

Comparison of generational effect on proteins and metabolites in non-transgenic and transgenic soybean seeds through the insertion of the cp4-EPSPS gene assessed by omics-based platforms

2020 ◽  
Vol 202 ◽  
pp. 110918
Author(s):  
Bruna K. de Campos ◽  
Rodrigo M. Galazzi ◽  
Bruna M. dos Santos ◽  
Tiago S. Balbuena ◽  
Fábio N. dos Santos ◽  
...  
Keyword(s):  
Soybean Seeds ◽  
Transgenic Soybean ◽  
Epsps Gene ◽  
Cp4 Epsps Gene ◽  
Cp4 Epsps

scholarly journals A Novel Mechanism for NF-κB-activation via IκB-aggregation: Implications for Hepatic Mallory-Denk-Body Induced Inflammation

2020 ◽  
Vol 19 (12) ◽  
pp. 1968-1985
Author(s):  
Yi Liu ◽  
Michael J. Trnka ◽  
Shenheng Guan ◽  
Doyoung Kwon ◽  
Do-Hyung Kim ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Nuclear Import ◽  
Cell Model ◽  
Protoporphyrin Ix ◽  
Zinc Protoporphyrin ◽  
Primary Hepatocytes ◽  
Protein Aggregate ◽  
Nuclear Entry ◽  
Antibody Recognition ◽  
Bona Fide

Mallory-Denk-bodies (MDBs) are hepatic protein aggregates associated with inflammation both clinically and in MDB-inducing models. Similar protein aggregation in neurodegenerative diseases also triggers inflammation and NF-κB activation. However, the precise mechanism that links protein aggregation to NF-κB-activation and inflammatory response remains unclear. Herein we find that treating primary hepatocytes with MDB-inducing agents (N-methylprotoporphyrin (NMPP), protoporphyrin IX (PPIX), or Zinc-protoporphyrin IX (ZnPP)) elicited an IκBα-loss with consequent NF-κB activation. Four known mechanisms of IκBα-loss i.e. the canonical ubiquitin-dependent proteasomal degradation (UPD), autophagic-lysosomal degradation, calpain degradation and translational inhibition, were all probed and excluded. Immunofluorescence analyses of ZnPP-treated cells coupled with 8 M urea/CHAPS-extraction revealed that this IκBα-loss was due to its sequestration along with IκBβ into insoluble aggregates, thereby releasing NF-κB. Through affinity pulldown, proximity biotinylation by antibody recognition, and other proteomic analyses, we verified that NF-κB subunit p65, which stably interacts with IκBα under normal conditions, no longer binds to it upon ZnPP-treatment. Additionally, we identified 10 proteins that interact with IκBα under baseline conditions, aggregate upon ZnPP-treatment, and maintain the interaction with IκBα after ZnPP-treatment, either by cosequestering into insoluble aggregates or through a different mechanism. Of these 10 proteins, the nucleoporins Nup153 and Nup358/RanBP2 were identified through RNA-interference, as mediators of IκBα-nuclear import. The concurrent aggregation of IκBα, NUP153, and RanBP2 upon ZnPP-treatment, synergistically precluded the nuclear entry of IκBα and its consequent binding and termination of NF-κB activation. This novel mechanism may account for the protein aggregate-induced inflammation observed in liver diseases, thus identifying novel targets for therapeutic intervention. Because of inherent commonalities this MDB cell model is a bona fide protoporphyric model, making these findings equally relevant to the liver inflammation associated with clinical protoporphyria.

scholarly journals Genomic Regions That Underlie Soybean Seed Isoflavone Content

2001 ◽  
Vol 1 (1) ◽  
pp. 38-44 ◽  
Author(s):  
K. Meksem ◽  
V. N. Njiti ◽  
W. J. Banz ◽  
M. J. Iqbal ◽  
My. M. Kassem ◽  
...  
Keyword(s):  
Linkage Group ◽  
High Performance ◽  
Biological Effects ◽  
Recombinant Inbred Lines ◽  
Soybean Seed ◽  
Soybean Seeds ◽  
Isoflavone Content ◽  
Seed Isoflavone ◽  
Genomic Regions

Soy products contain isoflavones (genistein, daidzein, and glycitein) that display biological effects when ingested by humans and animals, these effects are species, dose and age dependent. Therefore, the content and quality of isoflavones in soybeans is a key to their biological effect. Our objective was to identify loci that underlie isoflavone content in soybean seeds. The study involved 100 recombinant inbred lines (RIL) from the cross of ‘Essex’ by ‘Forrest,’ two cultivars that contrast for isoflavone content. Isoflavone content of seeds from each RIL was determined by high performance liquid chromatography (HPLC). The distribution of isoflavone content was continuous and unimodal. The heritability estimates on a line mean basis were 79% for daidzein, 22% for genistein, and 88% for glycitein. Isoflavone content of soybean seeds was compared against 150 polymorphic DNA markers in a one-way analysis of variance. Four genomic regions were found to be significantly associated with the isoflavone content of soybean seeds across both locations and years. Molecular linkage group B1 contained a major QTL underlying glycitein content (P=0.0001,R 2=50.2%), linkage groupNcontained a QTL for glycitein (P=0.0033,R 2=11.1%) and a QTL for daidzein (P=0.0023,R 2=10.3%) and linkage groupA1contained a QTL for daidzein (P=0.0081,R 2=9.6%). Selection for these chromosomal regions in a marker assisted selection program will allow for the manipulation of amounts and profiles of isoflavones (genistein, daidzein, and glycitein) content of soybean seeds. In addition, tightly linked markers can be used in map based cloning of genes associated with isoflavone content.

Improving metallomics information related to transgenic and non-transgenic soybean seeds using 2D-HPLC-ICP-MS and ESI-MS/MS

Metallomics ◽  
2012 ◽  
Vol 4 (4) ◽  
pp. 373 ◽  
Author(s):  
Lidiane Raquel Verola Mataveli ◽  
Mariana Fioramonte ◽  
Fabio César Gozzo ◽  
Marco Aurélio Zezzi Arruda
Keyword(s):  
Soybean Seeds ◽  
Transgenic Soybean ◽  
Esi Ms ◽  
Icp Ms

scholarly journals Discrimination of transgenic soybean seeds by terahertz spectroscopy

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Wei Liu ◽  
Changhong Liu ◽  
Feng Chen ◽  
Jianbo Yang ◽  
Lei Zheng
Keyword(s):  
Terahertz Spectroscopy ◽  
Soybean Seeds ◽  
Transgenic Soybean

Downstream process engineering evaluation of transgenic soybean seeds as host for recombinant protein production

2006 ◽  
Vol 32 (1) ◽  
pp. 7-12 ◽  
Author(s):  
Goran Robić ◽  
Cristiane S. Farinas ◽  
Elíbio L. Rech ◽  
Sônia M.A. Bueno ◽  
Everson A. Miranda
Keyword(s):  
Recombinant Protein ◽  
Recombinant Protein Production ◽  
Protein Production ◽  
Process Engineering ◽  
Soybean Seeds ◽  
Downstream Process ◽  
Transgenic Soybean

scholarly journals Elastin-like polypeptide and γ-zein fusions significantly increase recombinant protein accumulation in soybean seeds

2019 ◽  
Author(s):  
Jing Yang ◽  
Lu Niu ◽  
Hongli He ◽  
Yunqing Cheng ◽  
Xiaofang Zhong ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Total Protein ◽  
Oil Content ◽  
Total Soluble Protein ◽  
Protein Accumulation ◽  
Soybean Seeds ◽  
Mrna Levels ◽  
Transgenic Soybean ◽  
Protein Storage Vacuoles ◽  
Transgenic Lines

Abstract BackgroundSoybean seeds are an ideal host for the production of recombinant proteins because of their high content of proteins, long-term stability of seed proteins under ambient conditions, and easy establishment of efficient purification protocols. ResultsIn this study, a polypeptide fusion strategy was applied to explore the capacity of elastin-like polypeptide (ELP) and γ-zein fusions in increasing the accumulation of the recombinant protein in soybean seeds. Transgenic soybean plants were generated to express the γ-zein- or ELP-fused green fluorescent protein (GFP) under the control of the soybean seed-specific promoter BCSP. Significant differences were observed in the accumulation of zein-GFP and GFP-ELP from that of the unfused GFP in transgenic soybean seeds based on the total soluble protein (TSP), despite the low-copy of T-DNA insertions and similar expression at the mRNA levels in selected transgenic lines. The average levels of zein-GFP and GFP-ELP accumulated in immature seeds of these transgenic lines were 0.99% and 0.29% TSP, respectively, compared with 0.07% TSP of the unfused GFP. In mature soybean seeds, the accumulation of zein-GFP and GFP-ELP proteins was 1.8% and 0.84% TSP, an increase of 3.91- and 1.82-fold, respectively, in comparison with that of the unfused GFP (0.46% TSP). Confocal laser scanning analysis showed that both zein-GFP and GFP-ELP were deposited in the protein storage vacuoles of transgenic seeds, while the unfused GFP was mainly distributed in the cytoplasm. Despite increased recombinant protein accumulation, there were no significant changes in the total protein and oil content in seeds between the transgenic and non-transformed plants, suggesting the possible presence of threshold limits of total protein accumulation in transgenic soybean seeds. ConclusionsOverall, our results indicate that γ-zein and ELP fusions significantly increased the accumulation of the recombinant protein, but exhibited no significant influence on the total protein and oil content in soybean seeds.

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