Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Quantitative proteomic analysis of PVY-infected potato plants at normal and elevated temperature

ABSTRACT: To explore the underlying mechanisms that lead to increased susceptibility of potato cultivar Chicago to PVY at elevated (28°C) temperature compared with normal conditions (22°C), iTRAQ-based quantitative comparative proteomic analysis was conducted at 8 and 14 dpi

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Solanum Tuberosum (potato)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Igor Fesenko

LAB HEAD: Michael Taliansky

PROVIDER: PXD020495 | Pride | 2020-11-23

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	PVY22_14dpi.raw	Raw
	PVY22_8dpi.raw	Raw
	PVY28_14dpi.raw	Raw
	PVY28_8dpi.raw	Raw
	checksum.txt	Txt

Items per page:

1 - 5 of 6

Publications

Role of the methionine cycle in the temperature-sensitive responses of potato plants to potato virus Y.

Fesenko Igor I Spechenkova Nadezhda N Mamaeva Anna A Makhotenko Antonida V AV Love Andrew J AJ Kalinina Natalia O NO Taliansky Michael M

Molecular plant pathology 20201104 1

Plant-virus interactions are greatly influenced by environmental factors such as temperatures. In virus-infected plants, enhanced temperature is frequently associated with more severe symptoms and higher virus content. However, the mechanisms involved in such regulatory effects remain largely uncharacterized. To provide more insight into the mechanisms whereby temperature regulates plant-virus interactions, we analysed changes in the proteome of potato cv. Chicago plants infected with potato vir ...[more]

PMID: 33146443

Similar Datasets

Quantitative proteomic dataset of the moss Physcomitrium patens PpRALF knockout lines

Project description:RAPID ALKALINIZATION FACTOR (RALF) peptides are shown to regulate multiple physiological processes in plants, including modulation of immune response in angiosperms. This family of cysteine-rich peptide hormones has considerably expanded during land plant evolution, but the ancestral roles of RALF peptides in stress response remains poorly understood. Here, we used the moss Physcomitrium patens as a model to gain insight into the function of PpRALF peptides in response to abiotic and biotic stress factors in non-vascular plants. The quantitative proteomic analysis revealed cooperative down-regulation of M6 metalloproteases and membrane proteins, including those involved in stress response, in PpRALF1, 2 and 3 knockout (KO) lines.

2023-01-20 | PXD037111 | Pride

Tef (Eragrostis tef) iTRAQ-labelled protein fractions

Project description:The orphan crop, Eragrostis tef, was subjected to controlled drought conditions to observe the physiological parameters and proteins changing in response to dehydration stress. Physiological measurements involving electrolyte leakage, chlorophyll fluorescence and ultra-structural analysis showed tef plants to tolerate water loss to 50% RWC before adverse effects in leaf tissues were observed. Proteomic analysis using iTRAQ mass spectrometry and appropriate database searching enabled the detection of 5727 proteins, of which 211 proteins, including a number of spliced variants, were found to be differentially regulated with imposed stress conditions. Validation of the stress-related proteins, fructose-bisphosphate aldolase (FBA), glutamine synthetase (GLN) and the protective antioxidant proteins, monodehydroascorbate reductase (MDHAR) and peroxidase (POX), using immunodetection and enzymatic assay confirmed protein presence according to iTRAQ findings and showed increased protein abundance levels and enzymatic activity in response to water-deficit. GO-term enrichment and analysis revealed terms involved in biotic and abiotic stress response, signaling, transport, cellular homeostasis and pentose metabolic processes, to be enriched in tef up-regulated proteins, while terms linked to ROS-producing processes under water-deficit, such as photosynthesis and associated light harvesting reactions, manganese transport and homeostasis, the synthesis of sugars and cell wall catabolism and modification, to be enriched in tef down-regulated proteins.

2017-11-21 | PXD007907 | Pride

Effect of deletion of htpG on global proteomic profile of M. tuberculosis H37Rv

Project description:The main objective of this study is to understand the effect of deletion of htpG on protein expression profile of M. tuberculosis H37Rv. Whole cell lysates were prepared from 4 biological replicates of the wild-type control and the ∆htpG knockout strains by bead beating in 1X PBS containing protease inhibitors and subjected to 8-plex iTRAQ.

2023-07-20 | PXD039393 | Pride

p53 amyloid induced cellular transformation and tumor formation in the mouse xenograft model

Project description:p53 amyloid formation is predicted to be involved in cancer initiation, but the direct evidence of how altered p53 acts as an oncogene is lacking. Cells with p53 amyloids show enhanced survival, apoptotic resistance with increased proliferation and migration rates. Proteomic profiling of cells containing p53 aggregates suggests that p53 amyloid formation triggers aberrant expression of pro-oncogenes while downregulating the tumor-suppressive genes. We propose that wild-type p53 amyloid formation can potentially contribute to the initiation of tumor development.

2022-07-16 | PXD019498 | Pride

Peanut (Arachis hypogaea L.)-root- LC-MS/MS

Project description:The root proteomics of two cultivars differing in seed Cd accumulation, Fenghua 1 (F, low Cd cultivar) and Silihong (S, high Cd cultivar), were investigated under 0 (CK) and 2 μM Cd (Cd) conditions. The eight root proteins from two biological replicates of both peanut cultivars under Cd-free and Cd treated were obtained from iTRAQ experiments.

2019-03-19 | PXD012670 | Pride

Heat stress triggers protein secretion into the extracellular matrix of sorghum cell suspension cultures

Project description:Plants reprogram gene expression as an adaptive response to survive high temperatures. While the identity and functions of intracellular heat stress-responsive proteins have been extensively studied, the heat response of proteins secreted to the extracellular matrix is unknown. Here, we used Sorghum bicolor, a species adapted for growth in hot climates, to investigate the extracellular heat-induced responses. When exposed to 40 C for 72 h, heat-sensitive Arabidopsis cell suspension cultures died, while ICSB338 sorghum cell cultures survived by activation of a transcriptional response characterized by the induction of HSP70 and HSP90 genes. Quantitative proteomic analysis of proteins recovered from cell culture medium revealed specific heat stress-induced protein expression within the sorghum secretome. Of the 265 secreted proteins identified, 100 responded to heat, with the majority (85%) possessing a predicted signal peptide for targeting to the classical secretory pathway. The differentially expressed proteins have putative functions in detoxification (36%), metabolism (32%) and protein modifications (19%), while 13% are unclassified. Extracellular proteins play a vital role in cell-cell communications during stress adaptation. Our study reveals new insights into the adaptive response of sorghum to heat and provides a useful resource of extracellular proteins that could serve as targets for developing thermotolerant crops.

2020-10-29 | PXD021536 | Pride

Synthetic yeast genome project

Project description:The experiment aimed to study the proteome variation in a yeast strain (YS031), which chromosome II was artificially synthezied, compared with the wild type strain (BY4741). Proteins were extracted from the yeast cells and digested with trypsin. The peptides were label with iTRAQ, separated with 2D LC (SCX and RP) and detected with a Q-Exactive MS. Proteome identification and quantification were performed with Mascot2.3 and iQuant3.0.

2018-10-27 | PXD003435 | Pride

Multiplexed Quantitative Analyses Using Data-Dependent Acquisition Without Dynamic Exclusion for trace sample analysis

Project description:In this project, we applied our recently developed turboDDA method in the analysis of low amount of sample and iTRAQ labeled trace sample. Compared with standard data-ependent acquisition approach with dynamic exclusion, we detected improvment in spectral purity and quantification accuracy.

2024-01-26 | PXD042252 | Pride

Dosage compensation mass spectrometry in platypus, chicken and mouse

Project description:Gene dosage imbalance of heteromorphic sex chromosomes (XY or ZW) exists between the sexes, and with the autosomes. Mammalian X chromosome inactivation was long thought to imply a critical need for dosage compensation in vertebrates. However, mRNA abundance measurements that demonstrated sex chromosome transcripts are neither balanced between the sexes or with autosomes in monotreme mammals or birds brought sex chromosome dosage compensation into question. This study examines transcriptomic and proteomic levels of dosage compensation in platypus and chicken compared to mouse, a model eutherian species. We analyzed mRNA and protein levels in heart and liver tissues of chicken, mouse and platypus.

2024-07-30 | PXD040182 | Pride

Quantitative proteomic dataset of the moss Physcomitrium patens SMG1 KO mutant line

Project description:Here, we provide an isobaric tag for relative and absolute quantitation (iTRAQ)-based quantitative proteomic dataset of the moss Physcomitrium patens smg1 knockout line. The kinase SMG1 is one of the key components of the NMD system in many organisms, including plants. Several lines with a deleted SMG1 in a land Physcomitrium patens subsp. patens (“Gransden 2004”, Frieburg) were produced by James P. B. Lloyd [doi.org/10.1111/tpj.12329]. One of these lines, SMG1 KO mutant line 2, was used for this study. Protonemata of WT and mutant lines were grown in200 ml liquid BCD medium supplemented with 5 mM ammonium tartrate (BCDAT) during a 16-h photoperiod at 250C for 8 days [https://doi.org/10.1101/pdb.prot5136]. All experiments were performed in three biological replicates.

2021-11-02 | PXD029205 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data