Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Dynamic responses of barley root quantitative succinyl-proteome to short-term phosphate starvation and recovery

ABSTRACT: Improving phosphate (Pi) acquisition and utilization efficiency is a crucial challenge for the sustainability of agriculture worldwide. The understanding of plant how to response and cope with Pi-limitation, and its underlying molecular mechanisms is key to discovering strategies of efficient Pi acquisition and utilization. Barley (Hordeum vulgare L.) is one of the major cereal crops, has distinct advantage for studying mechanisms of tolerance of phosphorus deficiency due to low Pi demand. Recent studied reveal that post-translational modification (PTM) by phosphorylation, ubiquitination, and glycosylation are play important roles in cellular regulation the plant phosphate starvation response (PSR). Lysine succinylation occurs frequently in the proteins associated with metabolic pathways, which may participate in the regulation of the plant PSR process. However, succinylation precisely modulates the metabolic pathways of proteins in response to PSR in barley remain largely unknown.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Hordeum Vulgare (barley)

TISSUE(S): Root

SUBMITTER: Juncheng Wang

LAB HEAD: Wang juncheng

PROVIDER: PXD022052 | Pride | 2021-03-31

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	F9259LPScR1_D1CK6H_1_Slot2-37_1_2365.d.zip	Other
	F9259LPScR1_D1CK6H_2_Slot2-37_1_2366.d.zip	Other
	F9259LPScR1_D1CK6H_3_Slot2-37_1_2367.d.zip	Other
	F9259LPScR1_H1E_48H_1_Slot2-41_1_2381.d.zip	Other
	F9259LPScR1_H1E_48H_2_Slot2-41_1_2382.d.zip	Other

Items per page:

1 - 5 of 17

Similar Datasets

Dynamic responses of barley root quantitative succinyl-proteome to short-term phosphate starvation and recovery

Project description:Improving phosphate (Pi) acquisition and utilization efficiency is a crucial challenge for the sustainability of agriculture worldwide. The understanding of plant how to response and cope with Pi-limitation, and its underlying molecular mechanisms is key to discovering strategies of efficient Pi acquisition and utilization. Barley (Hordeum vulgare L.) is one of the major cereal crops, has distinct advantage for studying mechanisms of tolerance of phosphorus deficiency due to low Pi demand. Recent studied reveal that post-translational modification (PTM) by phosphorylation, ubiquitination, and glycosylation are play important roles in cellular regulation the plant phosphate starvation response (PSR). Lysine succinylation occurs frequently in the proteins associated with metabolic pathways, which may participate in the regulation of the plant PSR process. However, succinylation precisely modulates the metabolic pathways of proteins in response to PSR in barley remain largely unknown

2021-03-31 | PXD022053 | Pride

Dynamic responses of barley root quantitative succinyl-proteome to short-term phosphate starvation and recovery

2021-07-13 | PXD022077 | Pride

Phytoplasma induced changes in acetylatome and succinylatome provide evidence for involvement of acetylated proteins in Paulownia witches’ broom

Project description:Lysine acetylation and succinylation are post-translational modifications of proteins, and have been shown to play roles in plant response to pathogen infection. Phytoplasma infection can directly alter multiple metabolic processes in Paulownia and lead to Paulownia witches’ broom (PaWB), the major cause of Paulownia mortality worldwide. To explore the extent and function of lysine acylations during phytoplasma infection, we investigated global proteome, acetylome, and succinylome of phytoplasma-infected Paulownia tomentosa seedlings. In total, we globally yield 8963 proteins, 2893 acetylated, and 1271 succinylated proteins. Among them, 425 substrates were simultaneously acetylated and succinylated. Comparative analysis revealed that 276 proteins, 546 acetylated proteins and 5 succinylated proteins were associated with PaWB. Our results suggested that acetylation may be more important than succinylation in response to phytoplasma infection. Enzymatic assays showed that acetylation modified the activities of protochlorophyllide reductase and RuBisCO in phytoplasma-infected seedlings. On the basis of these results, a model to elucidate the molecular mechanism responses to PaWB was proposed and this research offer a resource for functional studies on the effects of acetylation on protein function.

2019-04-04 | PXD012701 | Pride

Succinylation in pseudorabies virus infection

Project description:We examined the global succinylation during PRV infection through a 4D label free quantitative proteomics method, which is the conventional separation of the three dimensions of mass-to-charge ratio, retention time, and ion intensity with the inclusion of the ion separation as a fourth dimension. We analyzed the function of some key enzymes that underwent succinylation and determine whether viral proteins undergo succinylation.

2023-03-02 | PXD040521 | Pride

A Qualitative Proteome-wide Lysine Succinylation Profiling of Tea Revealed Its Involvement in Primary Metabolism

Project description:Background: Lysine succinylation of proteins has potential impacts on protein structure and function, which occurred on post-translation level. However, the information about the lysine succinylation of proteins in tea plants is limited. In the present study, the significant signal of succinylation in tea plants was found by western blot. Subsequently, we performed qualitative analyses to globally identify lysine succinylation substrates by using high accuracy nano LC-MS/MS combined with affinity purification. Results: As a result, a total of 142 lysine succinylation sites were identified in 86 proteins. The identified succinylated proteins are involved in various biological processes and a large proportion of the succinylation sites are present on proteins in the primary metabolism pathway, including glyoxylate and dicarboxylate metabolism, the tricarboxylic acid (TCA) cycle and glycine, serine and threonine metabolism. Moreover, 10 new succinylated sites on histones were detected in tea plants either. Conclusions: These results suggested that succinylated proteins in tea plants might play critical regulatory roles in biological processes, especially in the primary metabolism. This study not only globally analysed the functional annotation of lysine succinylation in tea plants, but also provided valuable information for further investigating the functions of lysine succinylation in tea plants.

2022-02-23 | PXD011717 | Pride

GlobaGlobal involvement of lysine crotonylation in protein modification and transcription regulation in ricel involvement of lysine crotonylation in protein modification and transcription regulation in rice

Project description:Lysine crotonylation (Kcr) is a newly discovered post-translational modification (PTM) existing in mammalian. Here, we performed a global crotonylome analysis of rice (Oryza sativa L. japonica) using high accuracy nano-LC-MS/MS in combination with crotonylated peptide enrichment. A total of 1,265 lysine crotonylation sites were identified on 690 proteins in rice seedlings. Subcellular localization analysis revealed that 51% of the crotonylated proteins identified were predicted to be associated with chloroplasts. The photosynthesis-associated proteins were also mostly enriched in total crotonylated proteins. Furthermore, to assess the relevance between histone Kcr and the genome, we performed a genomic localization analysis of histone Kcr by ChIP-seq analysis. Of the 10,923 identified peak regions, the majority (86.7%) of the enriched peaks were located in genes, especially exons. Furthermore, the degree of histone Kcr modification was positively correlated with gene expression in genic regions. Compared with other published histone modification data, the Kcr was co-located with the active histone modifications. Interestingly, histone Kcr facilitated expression of genes with existing active histone modifications. In addition, 77% of histone Kcr modifications overlapped with DNase hypersensitive sites (DHSs) in intergenic regions of the rice genome, and might mark other cis-regulatory DNA elements which are different from IPA1, a transcription activator in rice seedling. Overall, our results provide a comprehensive understanding of the biological functions of the crotonylome and new active histone modification in transcriptional regulation in plants.

2018-07-23 | PXD008716 | Pride

DLST mutations in pheochromocytoma and paraganglioma cause proteome hyposuccinylation and metabolic remodeling

Project description:Using stable cell lines, we found that succinylation levels were highly dependent on DLST. Furthermore, PPGL-causing DLST mutations, predicted to alter DLST homo-oligomeric complex structure, caused a significant remodeling of the cellular succinylome. Succinylation is thought to cause major chemical and structural changes in proteins, most likely influencing their function. Accordingly, we found that the dysregulation of succinylation appeared to influence several essential pathways related to PPGL development such as hypoxia, glycolysis and oxidative phosphorylation. This study points to succinylation as a new mechanism involved in the development of PPGLs, supporting the growing body of research highlighting the role of this PTM in different types of cancer.

2023-05-04 | PXD036782 | Pride

Human cell LC-MS shows phosphorylation sites of stathmin

Project description:HIV gp120-induced stathmin phosphorylation peptide sequences identified by mass spectrometry in the proteins immunoprecipitated from stathmin-GFP expressed cell lysates with the GFP-beads.

2021-09-10 | PXD023868 | Pride

Histone lysine acetylation, butyrylation, and crotonylation dynamics and functional interplay in rice under starvation and submergence

Project description:Histone lysine acylations are regulated by primary metabolism in animal cells. However, histone non-acetyl acylation is not yet studied in plants that have distinct primary metabolic pathways. In this work, we detected rice histone lysine butyrylation (Kbu) and crotonylation (Kcr) sites by mass spectrometry, and found both similar and specific acylation patterns compared with that in mammalian cells.

2018-09-06 | PXD009091 | Pride

Quantitative analysis of acetylation in Vero cells infected with Peste des petits ruminants virus

Project description:Peste des petits ruminants virus (PPRV) is a negative-stranded RNA virus belonging to the Paramyxoviridae family and causes acute, highly contagious disease in small ruminants. Lysine acetylation plays central role in regulating gene expression. However, the extent and function of lysine acetylation in host cells during PPRV infection remains unknown. In this study, intensive proteomic quantification analysis of the proteome and acetylome of PPRV-infected Vero cells was performed using dimethylation labeling-based quantitative proteomics. As results, we identified 4729 proteins and 1068 acetylated proteins with 2641 quantified modification sites detected by mass spectrometry, of which 304 acetylated proteins with 410 acetylation sites were significantly acetylated in response to PPRV infection. Bioinformatics analyses revealed that the differentially acetylated proteins participated in carbohydrate catabolic and DNA metabolic process, and were associated with multifarious functions, suggesting that intracellular activities were extensively changed after PPRV infection. Protein-protein interaction network of the identified proteins further indicated that a variety of chaperone and ribosome processes were modulated by acetylation. To our knowledge, this is the first study on acetylome in host cell infected with PPRV. It provides an important point for future studies on the acetylated proteins involved in the host response to PPRV replication.

2023-10-24 | PXD025081 | Pride