Browse
Submit Data
Databases
API
Help

Dataset Information

356 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Pitcher fluid protein profiling of Nepenthes x ventrata

ABSTRACT: We studied protein profile in the first three days upon pitcher opening to understand carnivory trait of Nepenthes x ventrata. The proteome analysis of pitcher fluid from N. × ventrata was performed by mass spectrometry (nLC-MS/MSALL).

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Nepenthes Ventricosa X Nepenthes Alata

TISSUE(S): Pitcher Secretion

SUBMITTER: Hoe-Han Goh

LAB HEAD: Hoe-Han Goh

PROVIDER: PXD007251 | Pride | 2017-08-14

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	C1.wiff	Wiff
	C1.wiff.scan	Wiff
	C2.wiff	Wiff
	C2.wiff.scan	Wiff
	C3.wiff	Wiff

Items per page:

1 - 5 of 14

Publications

Proteomic analysis of pitcher fluid from Nepenthes × ventrata.

Wan Zakaria Wan Nor Adibah WNA Aizat Wan Mohd WM Goh Hoe-Han HH Noor Normah Mohd NM

Data in brief 20180202

The carnivorous plants of genus Nepenthes produce unique pitchers containing secretory glands, which secrete proteins into the digestive fluid. We investigated protein profile in the pitcher fluid during the first three days of opening to understand carnivory trait of Nepenthes × ventrata. The proteome analysis of pitcher fluid from N. × ventrata was performed by label-free quantitative liquid chromatography mass spectrometry (nLC-MS/MSALL). Raw MS d ...[more]

PMID: 29876422

Publication: 1/3

Similar Datasets

Pitcher fluid protein profiling of Nepenthes ampullaria

Project description:We studied protein profile in the first three days upon pitcher opening to understand carnivory trait of Nepenthes ampullaria. The proteome analysis of pitcher fluid was performed by mass spectrometry analysis using Thermo Easy-nLC Orbitrap Fusion Tribid MS. Analysis was performed in pools of 6 pitchers for each species and analysed in 3 technical replicates each.

2019-08-28 | PXD011893 | Pride

Carbonylation proteome of rice embryo

Project description:Using affinity chromatography to enrich carbonylated proteins from rice embryos germinated for 0, 24, 48, 72 h. Sequential window acquisition of all therotical spectra (SWATH) technology was used to quantify carbonylated proteins. Mass spectra data was searched to discover carbonylated peptides and their corresponding proteins.

2016-02-01 | PXD001429 | Pride

Venoms for all occasions: the functional toxin profiles of different anatomical regions in sea anemones are related to their ecological function

Project description:Phylum Cnidaria is the oldest extant venomous group and is defined by the presence of nematocysts, specialised organelles responsible for venom production and delivery. While nematocysts and toxin peptides are distributed across the entire animal, nematocyst and venom profiles have been shown to differ across morphological structures in actiniarians. In this study, we explore the relationship between patterns of toxin expression and the ecological roles of discrete anatomical structures in Telmatactis stephensoni. Specifically, using a combination of proteomic and transcriptomic approaches, we examined whether there is a direct correlation between the functional similarity of regions and the similarity of their associated toxin expression profiles. We report that the regionalisation of toxin production is consistent with the partitioning of the ecological roles of venom across envenomating structures, and that three major functional regions are present in T. stephensoni— tentacles, epidermis and gastrodermis. Additionally, we find that structures which serve similar functions not only have comparable toxin profiles but also similar nematocyst types. There was no overlap in the toxins identified using proteomics and transcriptomics, however, the expression patterns of specific milked venom peptides were conserved across RNA-seq and mass spectrometry imaging datasets. Furthermore, based on our data, it appears that acontia of T. stephensoni may be transcriptionally inactive and only mature nematocyst are present in the distal portions of the threads. Overall, we find that the venom profile of different anatomical regions in sea anemones varies according to its ecological functions.

2022-05-30 | PXD029717 | Pride

Identification of TbUnc119-interacting proteins by proximity-based biotinylation

Project description:Both intraflagellar transport (IFT) and lipidated intraflagellar transport (LIFT) pathways are essential for cilia/flagella biogenesis, motility and sensory functions. In the LIFT pathway, lipidated cargoes are transported into the cilia through the coordinated actions of cargo carrier proteins such as Unc119 or PDE6δ, as well as small GTPases Arl13b and Arl3 in the cilium. Our previous studies revealed a single Arl13b ortholog in the evolutionarily divergent Trypanosoma brucei. TbArl13 catalyses two TbArl3 homologs, TbArl3A and TbArl3C, suggesting the presence of a conserved LIFT pathway in these protozoan parasites. Only a single homolog to the cargo carrier protein Unc119 was identified in T. brucei genome, but its function in lipidated protein transport has not been characterized. In this study, we exploited the proximity-based biotinylation approach to identify binding partners of TbUnc119 using an improved version of biotin ligase BioID2. The BioID2 tag was fused to either the N-terminus (3HA-BioID2-TbUnc119) or the C-terminus (TbUnc119-BioID2-HA) of TbUnc119 and expressed using a cumate-inducible expression system in the procyclic cells of T. brucei. We performed LC-MS/MS on the affinity-purified biotinylated samples followed by evaluation of emPAI score.

2020-06-25 | PXD019488 | Pride

Macrophage proteome in response to Mycobacterium tuberculosis infection

Project description:This study investigates the proteomic alterations in human monocytic cell line (THP1) subsequent to infection with different strains of mycobacterium tuberculosis (H37Ra, H37Rv, BND433 and JAL2287) using the SWATH-MS strategy. THP1 proteome was analysed after 6, 18, 30 and 42 hours of infection with each strains and compared to that of uninfected cells. Our findings reveal temporal regulation of host response subsequent to Mtb infection.

2020-09-23 | PXD009046 | Pride

Macrophage proteome in response to Mycobacterium tuberculosis infection

2021-01-05 | PXD022352 | Pride

Stn1 S74 phosphorylation - Telomeres, the protective ends of eukaryotic chromosomes, are replicated through concerted actions by conventional DNA polymerases and telomerase, though the regulation of this process is not fully understood

Project description:Publication abstract: Telomeres, the protective ends of eukaryotic chromosomes, are replicated through concerted actions by conventional DNA polymerases and telomerase, though the regulation of this process is not fully understood. Telomere replication requires (C)-Stn1-Ten1, a telomere ssDNA-binding complex that is homologous to RPA. Here, we show that the evolutionarily conserved phosphatase Ssu72 is responsible for terminating the cycle of telomere replication in fission yeast. Ssu72 controls the recruitment of Stn1 to telomeres by regulating Stn1 phosphorylation at S74, a residue that lies within the conserved OB fold domain. Consequently, ssu72Δ mutants are defective in telomere replication and exhibit long 3′ overhangs, which are indicative of defective lagging strand DNA synthesis. We also show that hSSU72 regulates telomerase activation in human cells by controlling the recruitment of hSTN1 to telomeres. Thus, in this study, we demonstrate a previously unknown yet conserved role for the phosphatase SSU72, whereby this enzyme controls telomere homeostasis by activating lagging strand DNA synthesis, thus terminating the cycle of telomere replication. Summary of MS experiment: Stn1 protein was tagged in the C-terminus with 13-myc tag and purified by immunoprecipitation. The purified extracts were separated by SDS-PAGE and proteins between 63 and 75 kDa were excised and in-gel digested. Tryptic peptides were analyzed by LC-MS/MS using an AB Sciex TripleTOF 6600 mass spectrometer upon separation by nanoLC-MS using an Ekspert 425 nanoLC with cHiPLC. Stn1 protein was identified with 48% of coverage and Serine-74 was found to be phosphorylated.

2019-02-19 | PXD011953 | Pride

Protein idetification by using DNA pull-down & MS assay

Project description:Identification of proteins binding to the promoter of hrpR gene in Pseudomonas syringae using DNA pull-down & MS assay

2021-03-23 | PXD023722 | Pride

Matrisome remodelling during Intervertebral Disc development and ageing

Project description:Intervertebral disc (IVD) is often the cause of low back pain. Degeneration occurs with age and is accompanied by extracellular matrix (ECM) depletion, culminating in nucleus pulpous (NP) extrusion and IVD destruction. Although the changes that occur with ageing in the IVD have been under study, not much attention has been given to ECM remodelling during normal development. Therefore, a thorough study of ECM composition and a comprehensive view on how this microenvironment is affected in normal ageing conditions is needed, to better understand the processes involved in IVD development and in age-associated degeneration. We have compared the NP matrisome of bovine IVDs from foetus, young and old animals by quantitative iTRAQ LC-MS/MS. Protein expression levels of the most interesting candidates were validated by Western Blot analysis. In total, 161 bovine proteins were identified. Of these, 77 molecules were common to the three different age groups, of which 36 defined the NP matrisome. Differential expression levels obtained for Collagen Type XI, XII, XIV, Fibronectin and Prolargin were independently confirmed. Herein, we demonstrate a shift in NP matrisome signatures that occurs in healthy bovine IVDs with development and ageing. Thus, this study provides insight into factors that may explain age-associated IVD degeneration, and which are putative targets for therapy. It also highlights key molecules, characteristic of early developmental stages, which constitute potential effectors in IVD regeneration.

2017-09-25 | PXD004922 | Pride