PXD027229 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Characterisation of the free and membrane-associated fractions of the thylakoid lumen proteome in Arabidopsis thaliana |
Description | In plants chloroplasts, the lumen of the thylakoid membrane houses proteins that are vital for photosynthetic electron transport, including water-splitting at photosystem (PS) II and shuttling of electrons from cytochrome b6f to PSI. Other lumen proteins maintain photosynthetic activity through biogenesis and turnover of PSII complexes. Although all lumen proteins are soluble, these known details have highlighted interactions of some lumen proteins with thylakoid membranes or thylakoid-intrinsic proteins. Meanwhile, the functional details of most lumen proteins, as well as their distribution between the soluble and membrane-associated lumen fractions, remain unknown. The current study isolated the soluble free lumen (FL) and membrane-associated lumen (MAL) fractions from Arabidopsis thaliana, and used gel- and mass spectrometry-based proteomics methods to analyse the contents of each proteome. These results identified lumenal proteins, and clearly distinguished the difference between the FL and MAL proteomes. The most abundant proteins in the FL fraction were involved in PSII assembly and repair, while the MAL proteome was enriched in proteins that support of the oxygen-evolving complex (OEC). Novel proteins, including a new PsbP domain-containing isoform, as well as several novel post-translational modifications and N-termini, are reported, and bi-dimensional separation of the lumen proteome identified several potential multi-protein oligomers in the thylakoid lumen. |
HostingRepository | PRIDE |
AnnounceDate | 2021-07-30 |
AnnouncementXML | Submission_2021-07-30_05:02:15.922.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD027229 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Andrea Trotta |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | phosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-07-12 01:42:02 | ID requested | |
⏵ 1 | 2021-07-30 05:02:16 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Arabidopsis thaliana, photosynthesis, chloroplast, thylakoid lumen, post-translational modification |
Contact List
Eva-Mari Aro |
contact affiliation | Molecular Plant Biology, University of Turku, Finland |
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
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD027229
- Label: PRIDE project
- Name: Characterisation of the free and membrane-associated fractions of the thylakoid lumen proteome in Arabidopsis thaliana