PXD017382

PXD017382 is an original dataset announced via ProteomeXchange.

Title	How paired PSII-LHCII supercomplexes mediate the stacking of plant thylakoid membranes unveiled by integrative structural mass-spectrometry
Description	Photosynthesis drives all life on Earth by exploiting solar energy to split water molecules through the Photosystem (PS) II enzyme. In plant thylakoid membranes, PSII binds a modular set of light harvesting complexes (LHCII) to form different types of PSII-LHCII supercomplex (PSII-LHCIIsc). Plant PSII-LHCIIsc are localized in the stacked region of the thylakoid membranes called grana, from which they can be isolated in paired conformations of type (C2S2M2)x2 and (C2S2M)x2, with the two supercomplexes facing each other at their stromal surface. Although the atomic structure of PSII-LHCIIsc has recently been solved, there is still a lack of knowledge on their mutual interactions when facing each other within apposing thylakoid membranes, as well as their structural dynamics in response to light variations. The major challenges in the structural determination of the stromal interactions are posed not only by the dynamic nature of these over 2-megadalton assemblies, but also by the heterogeneity of the LHCII subunits and the high flexibility of their stromally exposed N-terminal loops. Here, we explored the potential of combining top-down mass spectrometry (TD-MS) and crosslinking mass spectrometry (XL-MS) to peek through the keyhole of the tight stromal gap between two facing supercomplexes, unveiling so far hidden structural details. A first goal of experiments was to identify the distinct sequence variants and proteoforms involved in PSII-LHCIIsc structural dynamics in response to light modulation. To investigate their structural interactions, we treated paired PSII-LHCIIsc isolated from the three light conditions with two complementary chemical cross-linkers, targeting different residues and producing partially overlapping distance restraints. Most interactions detected “in-vitro” on the isolated paired supercomplexes were further supported by XL-MS results obtained “in-situ” on the corresponding thylakoid membranes.
HostingRepository	PRIDE
AnnounceDate	2023-05-15
AnnouncementXML	Submission_2023-05-15_02:19:26.648.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	PascalAlbanese
SpeciesList	scientific name: Pisum sativum (Garden pea); NCBI TaxID: 3888;
ModificationList	acetylated residue
Instrument	Q Exactive HF; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2020-02-04 08:33:24	ID requested
1	2020-03-19 07:11:51	announced
⏵ 2	2023-05-15 02:19:27	announced	2023-05-15: Updated project metadata.

Albanese P, Tamara S, Saracco G, Scheltema RA, Pagliano C, How paired PSII-LHCII supercomplexes mediate the stacking of plant thylakoid membranes unveiled by structural mass-spectrometry. Nat Commun, 11(1):1361(2020) [pubmed]

ProteomeXchange project tag: EPIC-XS

submitter keyword: plant proteomics,Top-down RP-LC-MS/MS, acetylation, DSSO, PSII, EDC, photosystem, CX-MS, crosslinking, chlorophyll-binding proteins

RichardScheltema
contact affiliation	Utrecht University / Pharmaceutical Sciences Biomolecular Mass Spectrometry and Proteomics Padualaan 8 , 3584 CH Utrecht
contact email	R.A.Scheltema@uu.nl
lab head
PascalAlbanese
contact affiliation	Politecnico di Torino
contact email	pascal.albanese@polito.it
dataset submitter

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/2020/03/PXD017382

PRIDE project URI

• PRIDE
  1. PXD017382
     1. Label: PRIDE project
     2. Name: How paired PSII-LHCII supercomplexes mediate the stacking of plant thylakoid membranes unveiled by integrative structural mass-spectrometry