DNA-based pollen identification
Ontology highlight
ABSTRACT:
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR380478.fastq.gz | Fastqsanger.gz | |||
| ERR380479.fastq.gz | Fastqsanger.gz | |||
| ERR380480.fastq.gz | Fastqsanger.gz | |||
| ERR380481.fastq.gz | Fastqsanger.gz | |||
| ERR380482.fastq.gz | Fastqsanger.gz |
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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.
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Project description:Pollen DNA metabarcoding to characterize plant biodiversity within the Natura 2000 network.
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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.
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