Transcriptome analysis of differentially expressed genes in the feronia (fer-4) mutant
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA516444 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR8473211_1.fastq.gz | Fastqsanger.gz | |||
| SRR8473211_2.fastq.gz | Fastqsanger.gz | |||
| SRR8473212_1.fastq.gz | Fastqsanger.gz | |||
| SRR8473212_2.fastq.gz | Fastqsanger.gz | |||
| SRR8473213_1.fastq.gz | Fastqsanger.gz |
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Project description:FERONIA (FER) receptor kinase is a multifunctional regulator controlling myriad plant growth and developmental processes and interactions with the environment. We perform a RNA-seq analysis of genes differentially expressed in fer-4 mutant and observed significant changes of groups of genes previously characterized to be involved in AUXIN, ABA, ethylene and RALF1 signaling. The Results provide insight into the molecular mechanisms of FERONIA participation in regulating peptide and hormone signaling.
2020-06-30 | GSE125468 | GEO
Project description:The goal of this study was to determine transcriptional changes in the FERONIA mutant (fer) in Arabidopsis leaves
2022-04-04 | GSE143634 | GEO
Project description:FERONIA (FER) receptor kinase has a versatile role in plant growth and development, biotic and abiotic stress responses, and reproduction. To gain new insights into the molecular interplay of these processes and to identify new functions of FER, we carried out quantitative transcriptome, proteome, and phosphoproteome profiling of wild type (WT) and a loss-of-function fer mutant in Arabidopsis plants. Gene Ontology terms for hormone signaling, abiotic stress, and biotic stress were significantly enriched among mis-expressed transcripts, proteins, and/or mis-phosphorylated proteins, in agreement with FER’s known roles in these processes. Analysis of multi-omics data and subsequent experimental evidence identified previously unknown functions of FER in ER (Endoplasmic Reticulum) body formation, glucosinolate biosynthesis. FER functions through transcription factor NAI1 to mediate ER body. FER also negatively regulates indole glucosinolates biosynthesis, partially through NAI1. Furthermore, we found that a group of abscisic acid (ABA)-induced transcription factors are hypo-phosphorylated in the fer mutant and demonstrated that FER acts through ABI5 to negatively regulate the ABA response during germination. Our integrated-omics study therefore reveals novel functions of FER and provides new insights into the underlying mechanisms of FER function.
2022-04-04 | GSE191303 | GEO
Project description:In vertebrate muscle, loss of Dysferlin results in the activation of compensatory muscle gene expression, even at pre-pathological stages. We hypothesized that if C. elegans fer-1 is also expressed in muscle, then fer-1 mutant worms might also exhibit compensatory muscle gene expression. To test this hypothesis, we used Affymetrix microarrays to profile gene expression from synchronized wild type and fer-1 mutant adults. To improve the specificity of this approach, we profiled two well characterized loss-of-function fer-1 mutants (hc1ts and hc24ts) and considered genes that changed similarly in both mutants as fer-1-regulated transcripts.
2009-06-25 | GSE16753 | GEO
Project description:FERONIA (FER) is a plasma membrane-localized receptor-like kinase (RLK) that belongs to the Catharantus roseus RLK1-like (CrRLK1L) subfamily. FER serves as a potential cell wall sensor that regulates multiple phytohormones, including ABA, JA, SA, BR, auxin, and ethyl, but the underlying regulatory mechanisms are still largely unknown. To further understand how FER regulates downstream signaling pathway, we performed FER-interacting proteins via immunoprecipitation-mass spectrometry (IP-MS) assay generated from FER-GFP transgenic plants.
2024-09-14 | PXD047596 | Pride
Project description:Here we report that FERONIA (FER) integrates phyB-mediated light signaling pathway to control salt stress response. Mutation in phytochrome B (phyB) largely suppresses the dwarfism and leaf bleaching phenotype of fer-4 mutant under salt stress. FER interacts with and phosphorylates the N-terminal domain of phyB. Mutation in fer-4 or disruption of the FER-mediated phosphorylation sites of phyB at Ser106 and Ser227 leads to a retention of phyB in the photobodies under dark conditions, suggesting that FER-mediated phosphorylation accelerates the dark reversion of phyB. Interestingly, salt stress slows down the dark reversion of phyB via the inhibition of the kinase activity of FER, and mutation of phyB or overexpression of PIF5 attenuates the salt-induced growth inhibition. Together, our study indicates that the plasma membrane-localized FER determines the dark reversion rate of phyB in the nucleus via a signature of phosphorylation and thus coordinates the extracellular stress signals and nuclear outputs to dynamically control plant growth and survival under stress conditions.
2021-11-08 | GSE188335 | GEO
Project description:Differentially expressed genes following ARID1A depletion
| PRJNA477786 | ENA
Project description:FERONIA (FER) is a ubiquitious expressed and a plasma memberane-localized receptor-like protein kinase which modulate many biological functions. Elucidating the interacting proteins is the crucial step in understanding the molecular function of FER in regulating plant development. However, weak and transient interactions make identifying FER interacting proteins a challenge. Here, we adapted a novel proximity-based labelling technique, pupylation-based interaction tagging (PUP-IT), to label interacting proteins, subsequent enriched by affinity capture, and analyzed by liquid chromatography-coupled tandem mass spectrometery (LC-MS/MS) to profile FER interacting proteins. To perform a quick screen, a transient protoplasts expression system was conducted to identify interacting proteins in mesophyll cells. In addition, we generated a transgenic line that harboring a tagging substrate-inducible system and FER-ligase recombinant protein driven by a native promoter for surveying the interacting proteins in seedlings and flower organ. We introduce and prove the concept of PUP-IT tool designed to detect protein interactions of significance in plants.
2024-08-13 | PXD045546 | Pride
Project description:FERONIA (FER) is a ubiquitious expressed and a plasma memberane-localized receptor-like protein kinase which modulate many biological functions. Elucidating the interacting proteins is the crucial step in understanding the molecular function of FER in regulating plant development. However, weak and transient interactions make identifying FER interacting proteins a challenge. Here, we adapted a novel proximity-based labelling technique, pupylation-based interaction tagging (PUP-IT), to label interacting proteins, subsequent enriched by affinity capture, and analyzed by liquid chromatography-coupled tandem mass spectrometery (LC-MS/MS) to profile FER interacting proteins. To perform a quick screen, a transient protoplasts expression system was conducted to identify interacting proteins in mesophyll cells. In addition, we generated a transgenic line that harboring a tagging substrate-inducible system and FER-ligase recombinant protein driven by a native promoter for surveying the interacting proteins in seedlings and flower organ. We introduce and prove the concept of PUP-IT tool designed to detect protein interactions of significance in plants.
2024-08-13 | PXD052510 | Pride
Project description:The goal of this study was to determine protein abundance and phosphorylation changes in the FERONIA mutant (fer) in Arabidopsis leaves. Seeds were germinated on 1/2MS with constant light (24hr light) for 10 days. Then, plants were transferred to soil and grown under short day condition (8-hour light and 16-hour dark) at 22C for another 3 weeks (21 days). Samples were 4 weeks old when collected. Three biological replicates of WT as well as fer mutant rosette leaves were collected at 4 weeks. Proteins were extracted and processed into peptides using a phenol-FASP methods (https://doi.org/10.1002/pmic.201800220). Peptides were labeled with TMT6-plex reagents (WT 126, 127N, 128C; fer 129N, 130C, 131). Following TMT multiplexing phoshopeptides were enriched using Titanspere Phos-TiO 10 uM beads (GL science).
2020-01-14 | MSV000084804 | MassIVE