Properties of Photosystem II lacking the PsbJ subunit

Boussac, Alain; Sellés, Julien; Hamon, Marion; Sugiura, Masahiro

doi:10.1007/s11120-021-00880-w

Cited by 11 publications

(4 citation statements)

References 78 publications

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“…Notably, PsbJ, PsbY, and the three extrinsic subunits—PsbO, PsbV, and PsbU—were not found in the density map, suggesting that they are loosely bound and have been dissociated from the PSII core during purification. PsbJ is located between PsbK and PsbF, and the absence of this subunit may lead to the loss of Q B , Mn 4 CaO 5 cluster, and extrinsic subunits (PsbO, PsbV, and PsbU) ( 5 , 44 , 45 ). PsbY is located in the vicinity of PsbE and is easily lost during the process of sample purification ( 46 ).…”

Section: Resultsmentioning

confidence: 99%

Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll d –containing cyanobacterium

Shen,

Gao,

Tang

et al. 2024

Sci. Adv.

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Acaryochloris marina is a unique cyanobacterium using chlorophyll d (Chl d ) as its major pigment and thus can use far-red light for photosynthesis. Photosystem II (PSII) of A. marina associates with a number of prochlorophyte Chl-binding (Pcb) proteins to act as the light-harvesting system. We report here the cryo-electron microscopic structure of a PSII-Pcb megacomplex from A. marina at a 3.6-angstrom overall resolution and a 3.3-angstrom local resolution. The megacomplex is organized as a tetramer consisting of two PSII core dimers flanked by sixteen symmetrically related Pcb proteins, with a total molecular weight of 1.9 megadaltons. The structure reveals the detailed organization of PSII core consisting of 15 known protein subunits and an unknown subunit, the assembly of 4 Pcb antennas within each PSII monomer, and possible pathways of energy transfer within the megacomplex, providing deep insights into energy transfer and dissipation mechanisms within the PSII-Pcb megacomplex involved in far-red light utilization.

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Section: Resultsmentioning

confidence: 99%

Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll d –containing cyanobacterium

Shen,

Gao,

Tang

et al. 2024

Sci. Adv.

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“…Representative graphs of 4 technical replicates for each complex are shown. a) m/z range from 3,600 to 7,000; Annotation of the peaks was done according to [25,26]. Stars indicate modified peptides (see also SI Table 1).…”

Section: Resultsmentioning

confidence: 99%

Isolation of a novel heterodimeric PSII complex via strep-tagged PsbO

Lambertz

Meier-Credo

Kucher

et al. 2022

Preprint

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The multi-subunit membrane protein complex Photosystem II (PSII) catalyzes the light-driven oxidation of water and with this the initial step of photosynthetic electron transport in plants, algae, and cyanobacteria. Its biogenesis is coordinated by a network of auxiliary proteins that facilitate the stepwise assembly of individual subunits and cofactors, forming various intermediate complexes until fully functional mature PSII is present at the end of the process. In the current study, we purified PSII complexes from a mutant line of the thermophilic cyanobacterium Thermosynechococcus vestitus BP-1 in which the extrinsic subunit PsbO, characteristic for active PSII, was fused with an N-terminal Twin-Strep-tag. Three distinct PSII complexes were separated by ion-exchange chromatography after the initial affinity purification. Two complexes differ in their oligomeric state (monomeric and dimeric) but share the typical subunit composition of mature PSII. They are characterized by the very high oxygen-evolving activity of approx. 6,000 μmol O2 x (mg Chl x h)-1. Analysis of the third (heterodimeric) PSII complex revealed lower oxygen-evolving activity of approx. 3,000 μmol O2 x (mg Chl x h)-1 and manganese content of 2.7 (+/- 0.2) per reaction center compared to 3.7 (+/- 0.2) of fully active PSII. Mass spectrometry and time-resolved fluorescence spectroscopy further indicated that PsbO is partially replaced by Psb27 in this PSII fraction, thus implying a role in the repair of the complex.

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“…Putatively, the PsbJ subunit may be dissociated at an earlier step in the high light-adapted PSII complexes. The absence of PsbJ is usually related to the formation of an inhibited or intermediate form of PSII core [59][60][61] . Thus, we speculate that the release of PsbJ may be a signal for PSII to recruit PRF2 to the binding site so that it could induce the formation of a photoprotective state for PSII core.…”

Section: Discussionmentioning

confidence: 99%

Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii

Li,

You,

Pang

et al. 2024

Nat Commun

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Photosystem II (PSII) catalyzes water oxidation and plastoquinone reduction by utilizing light energy. It is highly susceptible to photodamage under high-light conditions and the damaged PSII needs to be restored through a process known as the PSII repair cycle. The detailed molecular mechanism underlying the PSII repair process remains mostly elusive. Here, we report biochemical and structural features of a PSII-repair intermediate complex, likely arrested at an early stage of the PSII repair process in the green alga Chlamydomonas reinhardtii. The complex contains three protein factors associated with a damaged PSII core, namely Thylakoid Enriched Factor 14 (TEF14), Photosystem II Repair Factor 1 (PRF1), and Photosystem II Repair Factor 2 (PRF2). TEF14, PRF1 and PRF2 may facilitate the release of the manganese-stabilizing protein PsbO, disassembly of peripheral light-harvesting complexes from PSII and blockage of the QB site, respectively. Moreover, an α-tocopherol quinone molecule is located adjacent to the heme group of cytochrome b559, potentially fulfilling a photoprotective role by preventing the generation of reactive oxygen species.

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Properties of Photosystem II lacking the PsbJ subunit

Cited by 11 publications

References 78 publications

Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll d –containing cyanobacterium

Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll d –containing cyanobacterium

Isolation of a novel heterodimeric PSII complex via strep-tagged PsbO

Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii

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