Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1018708 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR26105488_1.fastq.gz | Fastqsanger.gz | |||
| SRR26105488_2.fastq.gz | Fastqsanger.gz | |||
| SRR26105489_1.fastq.gz | Fastqsanger.gz | |||
| SRR26105489_2.fastq.gz | Fastqsanger.gz | |||
| SRR26105490_1.fastq.gz | Fastqsanger.gz |
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Project description:Mung bean (Vigna radiate) sprouts are a popular choice among sprouted vegetables in Asia. Currently, the impact of nitrogen sources on the growth of mung bean sprouts remains poorly understood, and the underlying biological mechanisms responsible for the observed nonlinear growth patterns at different nitrogen levels have yet to be elucidated. In this research, in addition to conventional growth monitoring and quality evaluation, a comparative proteomics method was applied to investigate the molecular mechanisms of mung bean in response to 0, 0.025, 0.05, 0.075, and 0.1% urea concentrations.Our results indicated that mung bean sprout height and yield increased with rising urea concentrations but were suppressed beyond theL3 level (0.075% urea). Nitrate nitrogen and free amino acid content rose steadily with urea levels, whereas protein content, nitrate reductase activity, and nitrite levels followed apeak-then-decline trend, peaking at intermediate concentrations. Differential expression protein analysis was conducted on mung bean sprouts treated with different concentrations of urea, and more differentially expressed proteins participated in the L3 urea concentration. Analysis of common differential proteins among comparison groups showed that the mung bean sprouts enhanced their adaptability to urea stress environments by upregulating chlorophyll a-b binding protein and cationic amino acid transporter and downregulating the levels of glycosyltransferase, L-ascorbic acid, and cytochrome P450.Theproteomic analysis uncovered the regulatory mechanisms governing these metabolic pathways, identifying 47 differentially expressed proteins (DEPs) involved in the biosynthesis of proteins, free amino acids, and nitrogen-related metabolites.
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Project description:Mung bean contains up to 25% of the protein, is one of the great sources of plant-based protein. Since many allergens also function as defense-related proteins, it is important to determine their abundance level in the high-yielding disease-resistant cultivars. In this study, for the first time, we compared the seed proteome of disease-resistant high-yielding mung bean cultivars developed by conventional breeding approach. Using label-free quantitative proteomic platform, we successfully identified and quantified a total of 1373 proteins. Comparative analysis between the high-yielding disease-resistant cultivar (MC5) and other three cultivars showed a total of 69 proteins were significantly altered in abundance and overlapped across the cultivars. Subsequent bioinformatic analysis of these altered proteins demonstrated that PDF1 (a defensin-like protein) exhibited high sequence similarity and epitope matching with the established peanut allergens (Ara h 12 and 13), indicating a potential mung bean allergen. Conversely, known mung bean allergen proteins such as Vig r 2, Vig r 4, LTP1, PR2, beta-Conglycinin, and Glycinin G4 showed no alternation in the MC5 compared to other cultivars. Taken together, our findings suggest that the known allergen profiles may not be impacted by the conventional plant breeding method to develop improved mung bean cultivars.
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