Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A RALF-like peptide EaF82 derived from Epipremnum aureum inhibits pollen development in Arabidopsis and tobacco

ABSTRACT: A RALF-like peptide EaF82 derived from Epipremnum aureum inhibits pollen development in Arabidopsis and tobacco

PROVIDER: PRJNA719729 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR14142024.fastq.gz	Fastqsanger.gz
	SRR14142025.fastq.gz	Fastqsanger.gz
	SRR14142026.fastq.gz	Fastqsanger.gz
	SRR14142027.fastq.gz	Fastqsanger.gz
	SRR14142028.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 36

Similar Datasets

A RALF-like peptide EaF82 derived from Epipremnum aureum inhibits pollen development in Arabidopsis and tobacco

Project description:To investigate the function of previously cloned novel cysteine-rich peptide EaF82 which biochemical properties are similar to the Rapid Alkalinization Factor (RALF), we overexpressed EaF82 gene in Arabidopsis and found defects only in the pollen development. To further determine the affected genes and biological pathways, we compared the transcriptome profilings of two independent Arabidopsis EaF82 overexpressing lines (TA and TB) with that of the vector control line (C). The RNAseq analysis results revealed decreased expressions of five endogenous clade IV AtRALFs and genes responsible for cell wall modifications and pollen maturation, supporting the observed pollen abortion.

2021-04-06 | GSE171459 | GEO

Epipremnum aureum

Project description:Epipremnum aureum Organism overview

| PRJNA307464 | ENA

Epipremnum aureum

Project description:Epipremnum aureum Transcriptome or Gene expression

| PRJNA286034 | ENA

Tobacco pollen sequestrome dynamics

Project description:Tobacco pollen sequestrome dynamics

| PRJNA472708 | ENA

Epipremnum aureum

Project description:Epipremnum aureum under nature condition Raw sequence reads

| PRJNA851036 | ENA

Phosphoproteomics profiling of tobacco mature pollen and pollen activated in vitro

Project description:Tobacco mature pollen has extremely desiccated cytoplasm, and is metabolically quiescent. Upon re-hydration it becomes metabolically active and that results in later emergence of rapidly growing pollen tube. These changes in cytoplasm hydration and metabolic activity are accompanied by protein phosphorylation. In this study, we subjected mature pollen, 5-min-activated pollen, and 30-min-activated pollen to TCA/acetone protein extraction, trypsin digestion and phosphopeptide enrichment by titanium dioxide. The enriched fraction was subjected to nLC-MS/MS. We identified 471 phosphopeptides that carried 432 phosphorylation sites, position of which was exactly matched by mass spectrometry. These 471 phosphopeptides were assigned to 301 phosphoproteins, since some proteins carried more phosphorylation sites. Of the 13 functional groups, the majority of proteins were put into these categories: transcription, protein synthesis, protein destination and storage, and signal transduction. Many proteins were of unknown function, reflecting the fact that male gametophyte contains many specific proteins that have not been fully functionally annotated. The quantitative data highlighted the dynamics of protein phosphorylation during pollen activation; the identified phosphopeptides were divided into seven groups based on the regulatory trends. The major group comprised mature pollen-specific phosphopeptides that were dephosphorylated during pollen activation. Several phosphopeptides representing the same phosphoprotein had different regulation, which pinpointed the complexity of protein phosphorylation and its clear functional context. Collectively, we showed the first phosphoproteomics data on activated pollen where the position of phosphorylation sites was clearly demonstrated and regulatory kinetics was resolved.

2016-01-27 | PXD003042 | Pride

Arabidopsis CLE peptide hormones contribute to pollen development through precisely regulated transcriptomic and proteomic networks

Project description:The CLAVATA3/ESR-RELATED (CLE) peptide hormones are required for numerous plant growth and developmental processes. However, little is known regarding the function and working mechanism of the CLEs in the anther. Here, using RNA in situ hybridization analyses, we identified 7 CLE genes that are specifically expressed in the tapetum and microsporocytes in the anther, and the dominant-negative mutant plants of each of these genes exhibited significantly reduced anther size, pollen number, and abnormal pollen wall formation. Further transcriptomic and proteomic studies on cle19, DN-CLE19, and CLE19-OX mutant lines revealed that CLE19 affected the expression of more than 1,000 genes at the RNA level and 595 at the protein level, including genes involved in pollen coat and pollen exine formation, lipid metabolism, pollen germination, and hormone metabolism processes. Phenotypic analyses of mutants of the CLE19 downstream genes GRP20, ACOS5 and MEE48 revealed that the formation of pollen exine was affected in these mutants, confirming that these genes function downstream of CLE19 in the regulation of pollen wall formation. These findings demonstrate the function and downstream genes of CLE19 and redundant genes, providing insights into working pathways of the peptide hormones in pollen development.

2017-09-15 | GSE94607 | GEO

Tobacco pollen sequestrome dynamics

Project description:Transcriptome profiling of four RNA fractions in six developmental stages of tobacco (Nicotiana tabacum) male gametophyte

2018-05-24 | GSE114806 | GEO

Proteomic characterization of plasma membrane-enriched fraction from tobacco (Nicotiana tabacum L. cv Samsun) pollen tubes.

Project description:Pollen germination and subsequent pollen tube elongation are essential for successful land plant reproduction. These processes are achieved through well-documented activation of membrane trafficking and cell metabolism. Despite this, our knowledge of the dynamics of cellular phospholipids remains scarce. In this project, we analyzed the turnover of the glycerolipid composition during the establishment of cell polarity and elongation processes in tobacco pollen and described the proteo-lipid composition of pollen plasma membrane-enriched. To achieve this, we have combined several techniques, such as lipidomics, live-cell microscopy, and plasma membrane isolation coupled with mass spectrometry-based proteomic characterization.

2022-10-27 | PXD037046 | Pride

Proteomics of pollen development

Project description:Pollen development in angiosperms is one of the most important processes controlling plant reproduction and therefore productivity. At the same time pollen development is highly sensitive to environmental fluctuations including temperature, drought and nutrition. Therefore pollen biology is a major focus in applied studies and breeding approaches for improving plant productivity in a globally changing climate. The most accessible developmental stages of pollen are the mature pollen and the pollen tubes and are, thus, most frequently analyzed. To reveal a complete quantitative proteome map we additionally addressed the very early stages analyzing 8 stages of tobacco pollen development from diploid microsporocytes, meioses, tetrads, microspores, polarized microspores, bipolar pollen and desiccated pollen to pollen tubes. A protocol for the isolation of the early stages was established. Proteins were extracted and analyzed by a new Gel-LC-MS fractionation protocol. In total, 3817 protein groups were identified. Quantitative analysis was performed based on peptide count. Exceedingly stage-specific differential protein regulation was observed during the conversion from the sporophytic to the gametophytic proteome. A map of highly specialized functionality for the different stages could be revealed from metabolic activity, pronounced differentiation of proteasomal and ribosomal protein complex composition up to protective mechanisms such as high levels of heat shock proteins in the very early stages of development.

2014-04-14 | PXD000469 | 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