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Title | High-Light versus Low-Light: Effects on Paired Photosystem II Supercomplex Structural Rearrangement in Pea Plants. |
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Journal, issue, pages | Int J Mol Sci, Vol. 21, Issue 22, Year 2020 |
Publish date | Nov 16, 2020 |
Authors | Alessandro Grinzato / Pascal Albanese / Roberto Marotta / Paolo Swuec / Guido Saracco / Martino Bolognesi / Giuseppe Zanotti / Cristina Pagliano / |
PubMed Abstract | In plant thylakoid membranes Photosystem II (PSII) associates with a variable number of antenna proteins (LHCII) to form different types of supercomplexes (PSII-LHCII), whose organization is ...In plant thylakoid membranes Photosystem II (PSII) associates with a variable number of antenna proteins (LHCII) to form different types of supercomplexes (PSII-LHCII), whose organization is dynamically adjusted in response to light cues, with the CS more abundant in high-light and the CSM in low-light. Paired PSII-LHCII supercomplexes interacting at their stromal surface from adjacent thylakoid membranes were previously suggested to mediate stacking. Here, we present the cryo-electron microscopy maps of paired CS and CSM supercomplexes isolated from pea plants grown in high-light and low-light, respectively. These maps show a different rotational offset between the two supercomplexes in the pair, responsible for modifying their reciprocal interaction and energetic connectivity. This evidence reveals a different way by which paired PSII-LHCII supercomplexes can mediate stacking at diverse irradiances. Electrostatic stromal interactions between LHCII trimers almost completely overlapping in the paired CS can be the main determinant by which PSII-LHCII supercomplexes mediate stacking in plants grown in high-light, whereas the mutual interaction of stromal N-terminal loops of two facing Lhcb4 subunits in the paired CSM can fulfil this task in plants grown in low-light. The high-light induced accumulation of the Lhcb4.3 protein in PSII-LHCII supercomplexes has been previously reported. Our cryo-electron microscopy map at 3.8 Å resolution of the CS supercomplex isolated from plants grown in high-light suggests the presence of the Lhcb4.3 protein revealing peculiar structural features of this high-light-specific antenna important for photoprotection. |
External links | Int J Mol Sci / PubMed:33207833 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 13.1 Å |
Structure data | EMDB-10865, PDB-6yp7: EMDB-10866: EMDB-10867: EMDB-10868: EMDB-10887: |
Chemicals | ChemComp-CHL: ChemComp-CLA: ChemComp-LUT: ChemComp-XAT: ChemComp-NEX: ChemComp-LHG: ChemComp-OEX: ChemComp-FE2: ChemComp-CL: ChemComp-PHO: ChemComp-BCR: ChemComp-PL9: ChemComp-SQD: ChemComp-BCT: ChemComp-DGD: ChemComp-LMG: ChemComp-HEM: |
Source |
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Keywords | PHOTOSYNTHESIS / Cryo-EM / photosystem II / High Light |