Plasma membrane proteomics of Arabidopsis responses to flagellin
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)
SUBMITTER: Gitta Coaker
PROVIDER: MSV000079639 | MassIVE | Wed Apr 06 19:13:00 BST 2016
REPOSITORIES: MassIVE
Similar Datasets
Project description:Plasma membrane proton pump maintains proton electrochemical gradient and provides energy to secondary transporters. Arabidopsis mutant plants with reduced proton pump activity grow normal under ideal growth conditions; however their growth are reduced compared with wildtype plants when placed under the conditions that stress on protonmotive force (high external pH or high external potassium).
2015-04-01 | GSE34202 | GEO
Project description:Plasma membrane proton pump maintains proton electrochemical gradient and provides energy to secondary transporters. Arabidopsis mutant plants with reduced proton pump activity grow normal under ideal growth conditions; however their growth are reduced compared with wildtype plants when placed under the conditions that stress on protonmotive force (high external pH or high external potassium). Seedlings of wildtype, aha1, and aha2 mutant plants were grown under ideal growth condition. Total RNA from those seedlings were subjected to transcriptome analyses using Affymetrix Gene Chip.
2015-04-01 | E-GEOD-34202 | biostudies-arrayexpress
Project description:Plant leaf discs were treated with plant immunity elicitors (chitin or flg22) or water for 30 or 180 minutes
2020-05-19 | GSE150746 | GEO
Project description:Plasma Membrane Integrity Signaling
| PRJNA701242 | ENA
Project description:Membrane-associated, integral membrane and secreted proteins are of key importance in many cellular processes. For most of the 28 952 predicted proteins in Arabidopsis, the actual subcellular localisation has not been demonstrated experimentally. So far, their potential membrane-association has been deduced from algorithms that predict transmembrane domains and signal peptides. However, the comprehensiveness and accuracy of these algorithms is still limited. The majority of membrane-associated and secreted proteins is synthesised on membrane-bound polysomes. Therefore, the isolation and characterisation of mRNA associated with membrane-bound polysomes offers an experimental tool for the genome-wide identification of these proteins. Here we describe an efficient method to isolate mRNA from membrane-bound polysomes and report on the validation of the method to enrich for transcripts encoding membrane-associated and secreted proteins. The sensitivity and reproducibility of the isolation method was investigated by DNA microarray analysis. Pearson correlations between transcript levels obtained from three replicate isolations showed that the method is highly reproducible. A significant enrichment for mRNAs encoding proteins containing predicted transmembrane domains and signal peptides was observed in the membrane-bound polysomal fraction. In this fraction, 301 transcripts were classified by gene ontologies as âcellular component unknownâ, and potentially encode previously unrecognised secreted or membrane-associated proteins. Membrane-bound (MBP) and free polysomes (FP) were isolated in triplicate from one batch of two weeks old aboveground parts of Arabidopsis seedlings. Each combination of isolated MBP and FP was applied to 4 microarrays, of which two were dyeswapped, giving a total of 12 arrays.
2010-07-01 | E-GEOD-4023 | biostudies-arrayexpress
Project description:To understand the transcriptional response of mammalian cells to plasma membrane stress we induced partial loss of plasmid membrane integrity by chemogenetic induction of pore forming proteins (Gasderimin and MLKL) or treatment with the detergent digitonin. We monitored transcription with mRNAseq in the immediate hours after plasma membrane damage and identified conserved transcriptional programs.
2021-10-04 | GSE166538 | GEO
Project description:Membrane-associated, integral membrane and secreted proteins are of key importance in many cellular processes. For most of the 28 952 predicted proteins in Arabidopsis, the actual subcellular localisation has not been demonstrated experimentally. So far, their potential membrane-association has been deduced from algorithms that predict transmembrane domains and signal peptides. However, the comprehensiveness and accuracy of these algorithms is still limited. The majority of membrane-associated and secreted proteins is synthesised on membrane-bound polysomes. Therefore, the isolation and characterisation of mRNA associated with membrane-bound polysomes offers an experimental tool for the genome-wide identification of these proteins. Here we describe an efficient method to isolate mRNA from membrane-bound polysomes and report on the validation of the method to enrich for transcripts encoding membrane-associated and secreted proteins. The sensitivity and reproducibility of the isolation method was investigated by DNA microarray analysis. Pearson correlations between transcript levels obtained from three replicate isolations showed that the method is highly reproducible. A significant enrichment for mRNAs encoding proteins containing predicted transmembrane domains and signal peptides was observed in the membrane-bound polysomal fraction. In this fraction, 301 transcripts were classified by gene ontologies as ‘cellular component unknown’, and potentially encode previously unrecognised secreted or membrane-associated proteins. Keywords: mRNA localisation, mRNA fractionation, predict protein localisation
2006-03-17 | GSE4023 | GEO
Project description:Brassinosteroids (BRs) are endogenous plant hormones and essential for normal plant growth and development. MicroRNAs (miRNAs) of Arabidopsis thaliana are involved in mediating cell proliferation in leaves, stress tolerance, and root development. The specifics of BRs mechanisms involving miRNAs are unknown. To explore the role of miRNAs in BR-mediated pathways, we analyzed differences in miRNA profiles between control (mock solution) and 24-epibrassinolide (EBR) treatments from customized miRNA microarrays. Seedlings were separately cultured under exogenous 10 nM EBR treatments for 30 (EBR30) or 180 (EBR180) minutes, and total RNAs of all seedlings were extracted after seven days of growth. Two independent experiments were performed at each time (30 or 180 minutes).
2016-03-25 | E-GEOD-46377 | biostudies-arrayexpress
Project description:Using a previously identified small molecule inhibitor of the plant exocyst complex subunit EXO70A1, Endosidin2 (ES2), combined with a plasma membrane enrichment method and quantitative proteomic analysis, we examined the composition of plasma membrane proteins in the root of Arabidopsis seedlings, after inhibition of the ES2-targetted exocyst complex.
2023-05-18 | PXD037455 | Pride
Project description:Rab proteins are small GTPases that are important in the regulation of vesicle trafficking. RabA2b was identified through data mining to be stress responsive. Little is known about the involvement of RabA in plant responses to abiotic stresses. Promoter analysis of RabA2b showed strong activity during osmotic stress, which required ABA and was restricted to the vasculature. Sequence analysis of the promoter region identified predicted binding motifs for several ABA-responsive transcription factors. We cloned RabA2b and overexpressed it in Arabidopsis. The resulting transgenic plants were strikingly drought resistant. Subcellular localization studies detected strong colocalization between RabA2b and the plasma membrane (PM) marker PIP2. Further proteomic analysis of isolated PM fractions showed enrichment of stress-coping proteins as well as cell wall/cuticle modifiers in the transgenic lines. Finally, the cuticle permeability of transgenic leaves was significantly reduced compared to the wild type. Overall, these data provide new insights into the roles and modes of action of RabA2b during water stresses, and indicate that increased RabA2b mediated PM trafficking can affect the PM proteome and increase drought tolerance.
2022-02-15 | PXD028140 | Pride