PXD026183 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | STN7 kinase-dependent Light-harvesting complex (LHC) protein phosphorylations in the moss Physcomitrium (Physcomitrella) patens |
Description | Photosystem (PS) I and PSII enclose the reaction center subunits and cofactors responsible for the conversion of sunlight into chemical energy. In the thylakoid membrane of oxygenic photosynthetic organisms, PSII splits the water molecules and donates electrons to the electron transfer chain, and further via PSI to form NADPH. Proteins of the light-harvesting complexes (LHC) I and II are mainly associated with PSI and PSII, respectively, but also provide dynamics for the adjustments of the absorption cross-section of PSII and PSI upon changing light conditions. LHCII proteins N-terminal phosphorylation affects their interaction either with PSI or with PSII, and is a molecular mechanism present from green algae and early land plants to higher plants. The kinase STN7 is responsible for N-terminal phosphorylation of the LHCII proteins in algae and flowering plants model species, but the specific targets and role of STN7-dependent reversible phosphorylation in formation of various PS-LHC complexes in evolutionarily early land plants like mosses is poorly studied. The aim of this project was to identify the phosphorylated residues of the LHCII subunits of the moss Physcomitrium (Physcomitrella) patens (hereafter: P. patens), i.e. the LHCBM proteins, and to determine which of the phosphosites are phosphorylated by the STN7 kinase. Subsequently, the goal has been to identify which of the LHCBM subunits that are part of PSI-LHCI-LHCII complex (state complex), and of the moss-specific PSI-Large complex, are N-terminally phosphorylated in the STN7-dependent fashion. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:52:23.106.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD026183 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Andrea Trotta |
SpeciesList | scientific name: Physcomitrella patens subsp. patens (Moss); NCBI TaxID: 3218; |
ModificationList | phosphorylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-05-21 03:50:53 | ID requested | |
1 | 2022-06-24 00:13:58 | announced | |
⏵ 2 | 2023-11-14 08:52:23 | announced | 2023-11-14: Updated project metadata. |
Publication List
Keyword List
submitter keyword: Photosystem I, N-terminal phosphorylation,Physcomitrella patens, PSI-large, Physcomitrium patens, Light-harvesting complex II |
Contact List
Eva-Mari Aro |
contact affiliation | Molecular Plant Biology, University of Turku |
contact email | evaaro@utu.fi |
lab head | |
Andrea Trotta |
contact affiliation | Institute of Biosciences and Bioresources, National Research Council of Italy, Sesto Fiorentino (FI) |
contact email | andrea.trotta@utu.fi |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/06/PXD026183 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD026183
- Label: PRIDE project
- Name: STN7 kinase-dependent Light-harvesting complex (LHC) protein phosphorylations in the moss Physcomitrium (Physcomitrella) patens