photoinhibition / chloroplast stromal thylakoid / chloroplast photosystem II / plastoglobule / thylakoid lumen / plastid thylakoid membrane / chloroplast thylakoid / chloroplast thylakoid lumen / apoplast / photosystem II oxygen evolving complex ...photoinhibition / chloroplast stromal thylakoid / chloroplast photosystem II / plastoglobule / thylakoid lumen / plastid thylakoid membrane / chloroplast thylakoid / chloroplast thylakoid lumen / apoplast / photosystem II oxygen evolving complex / photosystem II assembly / thylakoid / protein phosphatase regulator activity / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / photosystem II / photosynthetic electron transport chain / chlorophyll binding / chloroplast stroma / poly(U) RNA binding / plastid / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / phosphate ion binding / chloroplast thylakoid membrane / photosynthesis / chloroplast / electron transfer activity / protein stabilization / iron ion binding / protein domain specific binding / mRNA binding / heme binding / metal ion binding / mitochondrion / cytosol Similarity search - Function
Photosystem II 5kDa protein, chloroplastic / Photosystem II PsbO, manganese-stabilising / Manganese-stabilising protein / photosystem II polypeptide / Photosystem II reaction centre M protein (PsbM) / Photosystem II PsbM superfamily / Photosystem II PsbM / Photosystem II PsbX / Photosystem II reaction centre X protein (PsbX) / Photosystem II PsbT / Photosystem II PsbL ...Photosystem II 5kDa protein, chloroplastic / Photosystem II PsbO, manganese-stabilising / Manganese-stabilising protein / photosystem II polypeptide / Photosystem II reaction centre M protein (PsbM) / Photosystem II PsbM superfamily / Photosystem II PsbM / Photosystem II PsbX / Photosystem II reaction centre X protein (PsbX) / Photosystem II PsbT / Photosystem II PsbL / Photosystem II CP43 reaction centre protein / Photosystem II PsbL superfamily / Photosystem II PsbT superfamily / Photosystem II CP43 reaction centre protein superfamily / Photosystem II reaction centre T protein / PsbL protein / Photosystem II PsbK / Photosystem II PsbK superfamily / Photosystem II 4 kDa reaction centre component / Photosystem II PsbI / Photosystem II CP47 reaction centre protein / Photosystem II PsbI superfamily / Photosystem II reaction centre I protein (PSII 4.8 kDa protein) / Photosystem II reaction centre protein H / Photosystem II protein D1 / Photosystem II reaction centre protein H superfamily / Photosystem II 10 kDa phosphoprotein / Photosystem II D2 protein / Photosystem II cytochrome b559, conserved site / Photosystem II cytochrome b559, alpha subunit / Photosystem II cytochrome b559, beta subunit / Photosystem II cytochrome b559, N-terminal / Photosystem II cytochrome b559, alpha subunit, lumenal region / Photosystem II cytochrome b559, alpha subunit superfamily / Cytochrome b559, alpha (gene psbE) and beta (gene psbF)subunits / Lumenal portion of Cytochrome b559, alpha (gene psbE) subunit / Cytochrome b559 subunits heme-binding site signature. / : / Photosystem antenna protein-like / Photosystem antenna protein-like superfamily / Photosystem II protein / Outer membrane protein/outer membrane enzyme PagP, beta-barrel / : / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. Similarity search - Domain/homology
Oxygen-evolving enhancer protein 1-1, chloroplastic / Photosystem II D2 protein / Photosystem II CP47 reaction center protein / Photosystem II CP43 reaction center protein / Cytochrome b559 subunit alpha / Photosystem II reaction center protein H / Photosystem II reaction center protein K / Photosystem II reaction center protein L / Photosystem II reaction center protein T / Cytochrome b559 subunit beta ...Oxygen-evolving enhancer protein 1-1, chloroplastic / Photosystem II D2 protein / Photosystem II CP47 reaction center protein / Photosystem II CP43 reaction center protein / Cytochrome b559 subunit alpha / Photosystem II reaction center protein H / Photosystem II reaction center protein K / Photosystem II reaction center protein L / Photosystem II reaction center protein T / Cytochrome b559 subunit beta / Photosystem II reaction center protein I / Photosystem II reaction center protein M / Photosystem II protein D1 / Photosystem II 5 kDa protein, chloroplastic / Expressed protein Similarity search - Component
Biological species
Arabidopsis thaliana (thale cress)
Method
single particle reconstruction / cryo EM / Resolution: 2.74 Å
Sven och Lilly Lawskis fond for naturvetenskaplig forskning
Sweden
Swedish Research Council
2020-03809
Sweden
Swedish Research Council
2024-04804
Sweden
Carl Trygger Foundation
CTS 19.324
Sweden
Kempe Foundation
JCK-2030
Sweden
Kempe Foundation
JCSMK24-599
Sweden
Citation
Journal: Photosynth Res / Year: 2026 Title: Effects of high light and elevated temperature on the structure of photosystem II isolated from Arabidopsis thaliana. Authors: Jack Forsman / André T Graça / Michael Hall / Wolfgang P Schröder / Johannes Messinger / Abstract: Photosystem II (PS II) is a large membrane-bound pigment-protein complex responsible for extracting electrons and protons from water during photosynthesis and releasing molecular oxygen into the ...Photosystem II (PS II) is a large membrane-bound pigment-protein complex responsible for extracting electrons and protons from water during photosynthesis and releasing molecular oxygen into the atmosphere. While light is required to drive the photochemical reactions, high light and high temperature can be damaging to PS II. To gain insight into potential structural consequences of such conditions, we performed an exploratory study where isolated PS II complexes (C2S2) from Arabidopsis thaliana were exposed to high light and elevated temperature and employed cryo-electron microscopy for structural determination. This resulted in a 'high light' structure (2.74 Å global resolution) which is compared to the published 2.44 Å structure of intact Arabidopsis-PSII vitrified under dim light conditions (control). The high light structure is missing several of the subunits present in the control, including the strongly bound light-harvesting antenna complexes as well as several small transmembrane and extrinsic subunits. Beyond the loss of subunits, the clearest evidence of specific photodamage was found on the acceptor side of the D1 and D2 subunits near the non-heme iron, including the loss of the bicarbonate ligand of the non-heme iron. Finally, we were able to observe that high light/elevated temperature conditions result in the movement of the D1:His252 residue, potentially forming a serine protease triad that may trigger auto-proteolysis of the D1 subunit.
Supramolecule #1: High-light exposed Photosystem II from Arabidopsis thaliana
Supramolecule
Name: High-light exposed Photosystem II from Arabidopsis thaliana type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#15 Details: Photosystem II from Arabidopsis thaliana was solubilised and isolated from the thylakoid membranes. The isolated particles were exposed to 30 min of high light (2000 uE) before plunge ...Details: Photosystem II from Arabidopsis thaliana was solubilised and isolated from the thylakoid membranes. The isolated particles were exposed to 30 min of high light (2000 uE) before plunge freezing and data collection
Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Details
Photosystem II particles were solubilised with n-dodecyl-B-matloside and seperated using sucrose gradients. Particles were washed and concentrated, beforebeing exposed to high light (2000 uE) for 30 mins before plunge freezing
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Electron microscopy
Microscope
TFS KRIOS
Specialist optics
Energy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV
Image recording
Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 15511 / Average exposure time: 2.17 sec. / Average electron dose: 40.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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