Browse
Submit Data
Databases
API
Help

Dataset Information

426 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Comparative proteomics of defense response to AAL toxin

ABSTRACT: A comparative proteomics analysis on AAL toxin treated jai1 mutant and its wild type revealed that JA pathway promoted AAL toxin induced PCD by regulating the relevant PCD components and/or through other hormone pathways in a SlCOI1 dependent manner.

Additional contact: Min Zhang, Zhejiang University.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Solanum Lycopersicum

TISSUE(S): Plant Cell, Leaf, Shoot

DISEASE(S): Wounds And Injuries

SUBMITTER: Jin Koh

LAB HEAD: Qiaomei Wang

PROVIDER: PXD002864 | Pride | 2016-06-27

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Book2.xlsx	Xlsx
	LTA1.mgf	Mgf
	LTA10.mgf	Mgf
	LTA10.mzid.gz	Mzid
	LTA10.pride.mgf.gz	Mgf

Items per page:

1 - 5 of 224

Publications

Critical Role of COI1-Dependent Jasmonate Pathway in AAL toxin induced PCD in Tomato Revealed by Comparative Proteomics.

Zhang Min M Koh Jin J Liu Lihong L Shao Zhiyong Z Liu Haoran H Hu Songshen S Zhu Ning N Dufresne Craig P CP Chen Sixue S Wang Qiaomei Q

Scientific reports 20160621

Alternaria alternata f.sp. Lycopersici (AAL) toxin induces programmed cell death (PCD) in susceptible tomato (Solanum lycopersicum) leaves. Jasmonate (JA) promotes AAL toxin induced PCD in a COI1 (coronatine insensitive 1, JA receptor)-dependent manner by enhancement of reactive oxygen species (ROS) production. To further elucidate the underlying mechanisms of this process, we performed a comparative proteomic analysis using tomato jasmonic acid insensitive1 ( jai1), the receptor mutant of JA, a ...[more]

PMID: 27324416

Similar Datasets

SIRT_mutant interactome - Comparative interactomes of SIRT6 and SIRTimplication of functional links to aging

Project description:In the present study, we identified SIRT6 (S56Y)- and SIRT7 (H187Y)-interacting proteins, and compared their interactomes to investigate functional links. Extra primary submitter: <a href="mailto:nglee@postech.ac.kr" target="_top">Namgyu Lee</a>, Department of Life Sciences, Pohang University of Science and Technology, Pohang, 790-784, Republic of Korea

2014-04-28 | PXD000850 | Pride

Arabidopsis thaliana LC-MS/MS in mock and AAL treated plants

Project description:AAL toxin (the major virulence factor of Alternaria alternata f. sp. lycopersici)was treated to wild type(Col-0)and transgenic Arabidopsis with enhanced GSH (AtECS1). A proteomic profile was obtained by nano LC-MS/MS analysis.Among the identified proteins, a few proteins were selected for qRT-PCR and western blot analysis. It was found that AAL mediated resistance in plants can be conferred by GSH through SA and ET mediated pathways, in addition to several stress responsive molecules.

2020-08-07 | PXD017124 | Pride

Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mTORC1 substrate

Project description:The serine/threonine kinase mammalian target of rapamycin (mTOR) governs growth, metabolism, and aging in response to insulin and amino acids (aa), and is often activated in metabolic disorders and cancer. Much is known about the regulatory signaling network around mTOR, but surprisingly few direct mTOR substrates have been established to date. To tackle this gap in our knowledge, we took advantage of a combined quantitative phosphoproteomic and interactomic strategy. We analyzed the insulin- and aa-responsive phosphoproteome upon inhibition of the mTOR complex 1 (mTORC1) component raptor, and analyzed in parallel the interactome of endogenous mTOR. By overlaying these two datasets, we identified acinus L as a potential novel mTORC1 target. We confirmed acinus L as a direct mTORC1 substrate by co-immunoprecipitation and MS-enhanced kinase assays. Our study delineates a triple proteomics strategy of combined phosphoproteomics, interactomics, and MS-enhanced kinase assays for the de novo-identification of mTOR network components, and provides a rich source of potential novel mTOR interactors and targets for future investigation. Additional contact details: <a href="mailto:k.thedieck@umcg.nl">Prof. Dr. Kathrin Thedieck</a> Department of Pediatrics, University of Groningen, University Medical Center Groningen (UMCG), 9713 AV Groningen, The Netherlands. Faculty VI - School of Medicine and Health Sciences, Carl von Ossietzky University Oldenburg, 26111 Oldenburg, Germany. Prof. Dr. Bettina Warscheid Faculty of Biology, Institute of Biology II, University of Freiburg, 79104 Freiburg, Germany. BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.

2015-04-28 | PXD001245 | Pride

Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mTORC1 substrate

2015-04-28 | PXD001196 | Pride

Spaceflight adaptation requires organ specific alterations in the proteomes of Arabidopsis

Project description:This experiment was launched on STS-129 in 2009 and was supported by NASA grant NNX07AH27G - Transgenic Plant Biomonitors of Space Flight Exposure to R.J. Ferl and A-L. Paul. Life in spaceflight demonstrates remarkable adaptive processes within the specialized environments of space vehicles which are subject to the myriad of attending and unique environmental issues associated with orbital trajectories. To examine the adaptive processes that occur in plants in space, leaves and roots from Arabidopsis seedlings that were grown from seed for 12 days on the International Space Station and preserved on orbit in RNAlater were returned to earth and analyzed using iTRAQ broad scale proteomics procedures.

2015-03-24 | PXD001179 | Pride

Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mTORC1 substrate

2015-04-28 | PXD001244 | Pride

SIRT6 and SIRT7 binding proteome

Project description:To find the SIRT6 and SIRT7 binding proteins, we expressed V5-tagged SIRT6 and SIRT7 and pulled down this protein with anti-V5 agarose affinity gel. Sirtuins are a family of NAD-dependent deacetylases which deacetylate not only histones but also a wide range of target proteins. Sirtuins are conserved from yeast to mammal, and are known to regulate many processes such as cellular metabolism, apoptosis, cellular senescence, cell cycle, and organism-level aging. Among the members of sirtuins showing different subcellular localization, SIRT1, SIRT6 and SIRT7 are localized in nucleus. Whereas many functions and interacting proteins of SIRT1 have been studied, functions of SIRT6 and SIRT7 are not extensively revealed yet. Since it is important to understand the molecular function of SIRT6 and SIRT7, we here aimed to identify interacting proteins in mammalian cells. Extra primary submitter: <a href="mailto:nglee@postech.ac.kr" target="_top">Namgyu Lee</a>, Department of Life Sciences, Pohang University of Science and Technology, Pohang, 790-784, Republic of Korea Lab head: <a href="mailto:kchoi@postech.ac.kr" target="_top">Kwan Yong Choi</a>, Department of Life Sciences and Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, 790-784, Republ ic of Korea

2014-04-28 | PXD000159 | Pride

O-fucosylated glycoproteins of Toxoplasma gondii

Project description:The fucose-binding Aleuria aurantia lectin (AAL) labels punctiform structures in proximity to the nuclei of Toxoplasma gondii tachyzoites. We have utilized AAL-lectin affinity purification in conjunction with LC MS/MS to identify a set of proteins modified with fucose on serines and threonines

2016-10-11 | PXD004426 | Pride

Voltage-Dependent Anion-Selective Channels and Other Mitochondrial Membrane Proteins Form Diverse Complexes in Beetroots Subjected to Flood-Induced Programmed Cell Death

Project description:In plants, programmed cell death (PCD) is involved in both the development and in the response to biotic and abiotic aggressions. In early stages of PCD, mitochondrial membranes are made permeable by the formation of permeability transition pores, whose protein composition is debated. Since flooding stress can produce PCD in several plant species, the first goal of this work was to know if flooding stress could be used to induce PCD in Beta vulgaris roots. To do this, two months old beet plants were flood-stressed from one to five days, and the alterations indicating PCD in stressed beetroot cells were observed with a confocal fluorescence microscope. In addition, cytochrome c was released from mitochondria. After assessing that flood stress induced PCD in beetroots, the composition of mitochondrial protein complexes was observed in control and flood-stressed beetroots. Protein complexes from isolated mitochondria were separated by native gel electrophoresis, and their proteins were identified by mass spectrometry. The spectra count of three isoforms of voltage-dependent anion-selective channels (VDAC) increased after one day of flooding. In addition, the size of the complexes formed by VDAC was higher in beetroots flood-stressed for one day (~200 kDa) compared with non-stressed ones (~100 kDa). Other proteins, like chaperonin CPN60-2, also formed complexes with different masses in control and flood-stressed beetroots. Finally, possible interactions of VDAC with other proteins were found performing a cluster analysis. These results indicate that mitochondrial protein complexes formed by VDAC could be involved in the process of programmed cell death in flood-stressed beetroots

2021-10-28 | PXD027781 | Pride

Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains

Project description:Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)- containing domain translocates ~90 A ̊ to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.Extra contact information:<a href="mailto:cusack@embl.fr">Stephen Cusack</a>, EMBL Grenoble Outstation, Unit of Virus Host-Cell Interactions, France ( corresponding author and lab head )

2016-01-04 | PXD002234 | Pride