PXD003042 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Phosphoproteomics profiling of tobacco mature pollen and pollen activated in vitro |
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. |
HostingRepository | PRIDE |
AnnounceDate | 2016-01-27 |
AnnouncementXML | Submission_2016-01-27_05:25:54.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Julia Maria Burkhart |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; scientific name: Nicotiana tabacum (Common tobacco); NCBI TaxID: 4097; |
ModificationList | monohydroxylated residue; phosphorylated residue |
Instrument | LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2015-10-12 23:56:19 | ID requested | |
⏵ 1 | 2016-01-27 05:25:55 | announced | |
Publication List
F, í, la J, Radau S, Matros A, Hartmann A, Scholz U, Fecikov, á J, Mock HP, Č, apkov, á V, Zahedi RP, Honys D, Phosphoproteomics Profiling of Tobacco Mature Pollen and Pollen Activated in vitro. Mol Cell Proteomics, 15(4):1338-50(2016) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Tabacco, pollen, phosphoproteomics |
Contact List
René Zahedi |
contact affiliation | Leibniz-Institut für Analytische Wissenschaften - ISAS - e.V. |
contact email | zahedi@isas.de |
lab head | |
Julia Maria Burkhart |
contact affiliation | Department of bioanalytics |
contact email | julia.burkhart@isas.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD003042
- Label: PRIDE project
- Name: Phosphoproteomics profiling of tobacco mature pollen and pollen activated in vitro