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Phosphoproteome Analysis In Developing Wheat Grains Under Different Nitrogen Conditions

ABSTRACT: Wheat (Triticum aestivum), one of the most important cereal crops, it provides many kinds of food for humans and animals, in this study, we performed the first comprehensive phosphoproteome analysis to study the regulatory mechanism of bread quality formation under different nitrogen fertilizer. Totally, 2470 phosphotides, represented 1372 proteins were identified in our study. and 411 proteins showed significant differences.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Triticum Aestivum (wheat)

TISSUE(S): Plant Cell, Seed

SUBMITTER: Shoumin Zhen

LAB HEAD: Yueming Yan

PROVIDER: PXD004128 | Pride | 2018-10-26

REPOSITORIES: Pride

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	A-Elute2-1.raw	Raw
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	A-Elute2-3.raw	Raw
	B-Elute2-1.raw	Raw
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Publications

Comparative Phosphoproteomic Analysis under High-Nitrogen Fertilizer Reveals Central Phosphoproteins Promoting Wheat Grain Starch and Protein Synthesis.

Zhen Shoumin S Deng Xiong X Zhang Ming M Zhu Gengrui G Lv Dongwen D Lv Dongwen D Wang Yaping Y Zhu Dong D Yan Yueming Y

Frontiers in plant science 20170130

Nitrogen (N) is a macronutrient important for plant growth and development. It also strongly influences starch and protein synthesis, closely related to grain yield and quality. We performed the first comparative phosphoproteomic analysis of developing wheat grains in response to high-N fertilizer. Physiological and biochemical analyses showed that application of high-N fertilizer resulted in significant increases in leaf length and area, chlorophyll content, the activity of key enzymes in leave ...[more]

PMID: 28194157

Similar Datasets

wheat seed phosphoproteome under water deficit

Project description:Drought is one of the most serious abiotic stresses, under which the crop yield is significantly reduced. Elite winter wheat cultivar Henong 341 (Triticum aestivum L.) was grown in experimental fields of China Hebei province (116°37′23″E, 37°41′02″N) Two different treatment conditions were designed: rain-fed (no water irrigation) and well-watered (water irrigation) conditions at jointing and flowering stages. Each treatment included three biological replicates and each plot was 25m2. In this study, a comprehensive phosphoproteomic analysis of developing grains of 26th day after flowering (DAF) in Chinese bread wheat cultivar Henong 341 under well-watered and water-deficit conditions was performed by means of TiO2 enrichment, LC/MS/MS analysis, and Label-free peptide-intensity quantification. Under well-watered conditions, a total of 590 unique phosphopeptides corresponding to 603 nonredundant phosphorylation sites, representing 471 phosphoproteins, were identified. While under water deficit, 63 unique phosphopeptides, corresponding to 61 phosphoproteins, were found to be differently regulated in phosphorylation status compared to well-watered conditions (≥2 fold intensities).

2016-07-09 | PXD000806 | Pride

New Insights into the Biosynthesis and Regulation of Wheat Amylose and Amylopectin from Proteomic and Phosphoproteomic Characterization of Granule-binding Proteins

Project description:Waxy starch has an important influence on bread dough and the qualities of breads. Generally, grain weight and yield in waxy wheat (Triticum aestivum L.) are significantly lower than in bread wheat. In this study, we performed the first proteomic and phosphoproteomic analyses of starch granule-binding proteins by comparing the waxy wheat cultivar Shannong 119 and the bread wheat cultivar Nongda 5181. The waxy and non-waxy wheats had similar starch granule morphological features and developmental patterns, and similar amylopectin quality in the grain. These results indicate that reduced amylose content does not affect amylopectin synthesis, but it causes significant reduction of total starch biosynthesis, grain size, weight and yield. Two-dimensional differential in-gel electrophoresis identified 40 differentially expressed protein (DEP) spots in waxy and non-waxy wheats, which belonged mainly to starch synthase (SS) I, SS IIa and granule-bound SS I. Most DEPs involved in amylopectin synthesis showed a similar expression pattern during grain development, suggesting relatively independent amylose and amylopectin synthesis pathways. Phosphoproteome analysis of starch granule-binding proteins, using TiO2 microcolumns and LC-MS/MS, showed that the total number of phosphoproteins and their phosphorylation levels in ND5181 were significantly higher than in SN119, but proteins controlling amylopectin synthesis had similar phosphorylation levels. Dynamic transcriptional expression profiling of starch biosynthesis-related genes indicated similar transcriptional expression profiles in both cultivars. Our results revealed that phosphorylation modifications played critical roles in amylose and amylopectin biosynthesis, but the lack of amylose did not affect the expression and phosphorylation of the starch granule-binding proteins involved in amylopectin biosynthesis.

2017-10-30 | PXD002805 | Pride

Wheat leaf phosphoproteome under drought stress

Project description:Waxy starch has an important influence on the qualities of breads. Generally, grain weight and yield in waxy wheat (Triticum aestivum L.) are significantly lower than in bread wheat. In this study, we performed the first proteomic and phosphoproteomic analyses of starch granule-binding proteins by comparing the waxy wheat cultivar Shannong 119 and the bread wheat cultivar Nongda 5181. These results indicate that reduced amylose content does not affect amylopectin synthesis, but it causes significant reduction of total starch biosynthesis, grain size, weight and grain yield. Two-dimensional differential in-gel electrophoresis identified 40 differentially expressed protein (DEP) spots in waxy and non-waxy wheats, which belonged mainly to starch synthase (SS) I, SS IIa and granule-bound SS I. Most DEPs involved in amylopectin synthesis showed a similar expression pattern during grain development, suggesting relatively independent amylose and amylopectin synthesis pathways. Phosphoproteome analysis of starch granule-binding proteins, using TiO2 microcolumns and LC-MS/MS, showed that the total number of phosphoproteins and their phosphorylation levels in ND5181 were significantly higher than in SN119, but proteins controlling amylopectin synthesis had similar phosphorylation levels. Our results revealed the lack of amylose did not affect the expression and phosphorylation of the starch granule-binding proteins involved in amylopectin biosynthesis.

2017-01-17 | PXD000646 | Pride

Comparative Phosphoproteome Analysis of Seedling Leaves in Brachypodium distachyon. under Different Drought Conditions

Project description:Drought stress is a major abiotic stress affecting plant growth and development. Brachypodiumdistachyon L. is a special model plant for wheat, barley, and several potential biofuel grasses. In this study, we make comparative phosphoproteome analysis of seeding leaves at the three leaf stage in Brachypodiumdistachyon L. for the different treatment conditions (6h, 24h). A total of 480 unique phosphopeptides, representing 439 phosphoproteins, were identified under drought stress. Motif-X analysis identified six motifs, such as [SP], [RxxS], [LxRxxS], [SxD], [SF] and [TP]. Molecular function and PPI analysis suggested that many proteins may take participation in signal transduction, gene expression, drought response and defense with energy metabolism and material transmembrane transport under moisture deficiency condition. Further analyses revealed that these SCPL phosphoproteins may play important roles in regulating signal transduction and material transmembrane transport to cope with the adverse environmental conditions. This study first focus on the effects of phosphorylation modification mechanisms on the growth and development of seeding leaves at different drought stresses.

2018-10-26 | PXD003522 | Pride

Phosphoproteomics of Jatropha curcas seedling under chilling stress

Project description:As a promising energy plant for biodiesel, Jatropha curcas is a tropical and subtropical shrub. Chilling is a major abiotic stress affecting the growth and development of J. curcas. In this study, we adopt the phosphoproteomic analysis, physiological measurement, ultrastructure observation to illustrate molecular mechanisms of J. curcas seedling under chilling (4 °C) stress. After chilling for 6 h, 308 significantly changed phosphoproteins were detected in J. curcas seedling without obvious physiological injury. When obvious physiological injury can be observed after chilling for 24 h, a total of 332 phosphoproteins were examined to be significantly changed, after recovery (28 °C) for 24 h, 291 phosphoproteins were varied at the phosphorylation level. The results of Gene Ontology analysis showed that phosphoproteins were mainly responsible for cellular protein modification process, transport, cellular component organization and signal transduction at the chilling and recovery periods. On the basis of protein-protein interaction network analysis, several protein kinases, such as SnRK2 (serine threonine-protein kinase srk2), MEKK1 (mitogen-activated protein kinase kinase kinase 1), EDR1, CDPK (calcium-dependent protein kinase), EIN2 (Ethylene-insensitive protein 2), EIN4, PI4K (phosphatidylinositol 4-kinase alpha 1) and 14-3-3 were possible responsible for cross-talk between ABA, Ca2+, ethylene, phosphoinositide and 14-3-3 mediated signaling pathways. We also highlighted the phosphorylation of HOS1 (E3 ubiquitin-protein ligase HOS1), APX (Cytosolic ascorbate peroxidase-1) and PIP2 (Aquaporin pip2) played vital roles in J. curcas seedling under chilling stress, and they will be valuable in further study form the molecular breeding perspective.

2019-01-09 | PXD011438 | Pride

Label-free quantitative phosphoproteomic profiling of cellular response induced by an insect cytokine paralytic peptide

Project description:Paralytic peptide (PP) participates in diverse physiological processions as an insect cytokine, such as immunity controls, paralysis induction, regulation of cell morphology and proliferation. To investigate the molecular mechanism underlying those physiological activities, we systematically investigated the global phosphorylation events in fat body of silkworm larvae induced by PP through label-free quantitative phosphoproteomics.

2017-01-02 | PXD004521 | Pride

Large-scale phosphoproteome analysis in seedling leaves of Brachypodium distachyon L

Project description:In this study, we carried out the first large-scale phosphoproteome analysis of seedling leaves in Brachypodium accession Bd21 using TiO2 microcolumns combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS) and MaxQuant software. A total, 1,470 phosphorylation sites in 950 phosphoproteins were identified. Of the 950 phosphoproteins identified, 127 contained 3 to 8 phosphorylation sites. The phosphoproteins and phosphosites identified in our study expanded our knowledge of protein phosphorylation modification in plants, especially in monocot.

2016-07-09 | PXD000868 | Pride

Quantitative proteomics and phosphoproteomics reveal that PIM3 modulates cell migration via regulating Rho GTPase signaling

Project description:For the phosphoproteomic analysis, three biological replicates and two technical replicates were analyzed, resulting in twelve data for quantification. Statistical analysis was performed using student’s t-test as described in details in the “LC-MS/MS and data analysis” section

2020-02-04 | PXD014044 | Pride

Citrullination of glucokinase is linked to autoimmune diabetes

Project description:Inflammation, including reactive oxygen species and inflammatory cytokines in tissues amplify various post-translational modifications (PTMs) of self-proteins. A number of PTMs have been identified as autoimmune biomarkers in the initiation and progression of Type 1 diabetes (T1D). In this study, we have identified the citrullination of pancreatic glucokinase (GK) as a result of inflammation, triggering autoimmunity and affecting GK biological functions. Glucokinase is expressed in hepatocytes to regulate glycogen synthesis, and in pancreatic beta cells as a glucose sensor to initiate glycolysis and insulin signaling. We identify autoantibodies and autoreactive CD4+ T cells to glucokinase epitopes in the circulation of T1D patients and NOD mice. Finally, citrullination alters GK biologic activity (Km) and suppresses glucose-stimulated insulin secretion. Our studies define glucokinase as a T1D biomarker, providing new insights of how inflammation drives PTMs to create both neoautoantigens and affect beta cell metabolism.

2022-03-17 | PXD028825 | Pride

Phosphoproteomic Analysis of Paper Mulberry under Chilling

Project description:Paper mulberry as a valuable woody species has a well chilling tolerance. In this study, phosphoproteomic analysis in combination with physiological measurement and mRNA quantification were employed to explore the molecular mechanism of chilling (4 °C) tolerance in paper mulberry. After chilling for 6 hours, there were 427 significant changed phosphoproteins detected in paper mulberry seedlings without obvious physiological injury. When obvious physiological injury occurred after chilling for 48 hours, a total of 611 phosphoproteins were found significantly change at phosphorylation level. According to 9 phosphorylation motifs extracted by Motif-X analysis, MAPKs, CDPKs, CDKs and CKs were considered as the primary upstream protein kinases. Results of GO analysis showed that phosphoproteins were mainly responsible for signal transduction, protein modification and translation during chilling. Additionally, transport and cellular component organization were respectively enriched after chilling for 6 and 48 hours. Based on the analysis of protein-protein interaction network, a protein kinases and phosphatases hub protein was thought as the key of phosphorylation regulation, which probably modulates cross-talk between Ca2+, BR, ABA and ethylene mediated signaling pathways. Together with results, we concluded a schematic chilling tolerance mechanism at phosphorylation level.

2018-04-20 | PXD005516 | Pride

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