The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis

Zhao, Ziyu; Vercellino, Irene; Knoppová, Jana; Sobotka, Roman; Murray, James W.; Nixon, Peter J.; Sazanov, L.A.; Komenda, Josef

doi:10.1101/2022.10.16.512410

Cited by 4 publications

(3 citation statements)

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“…We probed our fractions for six proteins involved in PSII assembly (Figure 2). HCF136, which acts very early in the assembly of D1 into the PSII reaction center (Meurer et al, 1998;Plücken et al, 2002;Zhao et al, 2023), was distributed among the refined margin, curvature, and stromal lamellae fractions, consistent with the prior localization of HCF136 to crude margins and stromal lamellae (Garcia-Cerdan et al, 2019). HCF244, OHP2, and RBD1 also mediate early steps in assembly of the PSII reaction center and had previously been localized to crude margin fractions (Knoppova et al, 2014;Hey and Grimm, 2018;Garcia-Cerdan et al, 2019;Li et al, 2019;Maeda et al, 2022;Calderon et al, 2023).…”

Section: Partitioning Of Proteins Involved In Thylakoid Membrane Biog...supporting

confidence: 70%

Localization of Proteins Involved in the Biogenesis of the Photosynthetic Apparatus to Thylakoid Subdomains in Arabidopsis

Chotewutmontri,

Barkan

2024

Preprint

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Thylakoid membranes in chloroplasts and cyanobacteria harbor the multisubunit protein complexes that catalyze the light reactions of photosynthesis. In plant chloroplasts, the thylakoid membrane system comprises a highly organized network with several subcompartments that differ in composition and morphology: grana stacks, unstacked stromal lamellae, and grana margins at the interface between stacked and unstacked regions. The localization of components of the photosynthetic apparatus among these subcompartments has been well characterized. However, less is known about the localization of proteins involved in the biogenesis and repair of the photosynthetic apparatus, the partitioning of proteins between two recently resolved components of the traditional margin fraction (refined margins and curvature), and the effects of light on these features. In this study, we analyzed the partitioning of numerous thylakoid biogenesis and repair factors among grana, curvature, refined margin, and stromal lamellae fractions of Arabidopsis thylakoid membranes, comparing the results from illuminated and dark-adapted plants. Several proteins previously shown to localize to a margin fraction partitioned in varying ways among the resolved curvature and refined margin fractions. For example, the ALB3 insertase and FtsH protease involved in photosystem II (PSII) repair were concentrated in the refined margin fraction, whereas TAT translocon subunits and proteins involved in early steps in photosystem assembly were concentrated in the curvature fraction. By contrast, two photosystem assembly factors that facilitate late assembly steps were depleted from the curvature fraction. The enrichment of the PSII subunit OE23/PsbP in the curvature fraction set it apart from other PSII subunits, supporting the previous conjecture that OE23/PsbP assists in PSII biogenesis and/or repair. The PSII assembly factor PAM68 partitioned differently among thylakoid fractions from dark-adapted plants and illuminated plants, and was the only analyzed protein to convincingly do so. These results demonstrate an unanticipated spatial heterogeneity of photosystem biogenesis and repair functions in thylakoid membranes, and reveal the curvature fraction to be a focal point of early photosystem biogenesis.

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Section: Partitioning Of Proteins Involved In Thylakoid Membrane Biog...supporting

confidence: 70%

Localization of Proteins Involved in the Biogenesis of the Photosynthetic Apparatus to Thylakoid Subdomains in Arabidopsis

Chotewutmontri,

Barkan

2024

Preprint

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“…We therefore propose that LHL4 binding to the PSII monomer during exposure to HL promotes the formation of an intermediate shielded form that protects the complex from photoinhibition. The structural mechanism is reminiscent of that recently proposed for the PSII oxygen-evolving complex, where the Ycf48 assembly factor binds to the PSII monomer, promoting the initial steps of PSII assembly in cyanobacteria (49).…”

Section: Resultsmentioning

confidence: 93%

Photoreceptor-induced LHL4 protects photosystem II inChlamydomonas reinhardtii

Dannay,

Bertin,

Cavallari

et al. 2024

Preprint

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Photosynthesis, the fundamental process using light energy to convert CO2to organic matter, is vital for life on Earth. It relies on capturing light through light-harvesting complexes in evolutionarily well-conserved photosystems (PS) I and II and on the conversion of light energy into chemical energy. Composition and organization of both photosystem core complexes are well conserved across evolution. PSII is particularly sensitive to photodamage but benefits from a large diversity of photoprotective mechanisms, finely tuned for the specific light conditions. Light Harvesting Complex protein family members (LHC and LHC-like families) have acquired a dual function during evolution. Members of the LHC antenna complexes of photosystems capture light energy whereas others dissipate excess energy that cannot be harnessed for photosynthesis. This process mainly occurs through non photochemical quenching (NPQ). In this work, we focus on the LHL4 protein, which is a LHC-like protein induced by UV-B and blue light photoreceptor signaling pathways in the model green microalgaeChlamydomonas reinhardtii. We demonstrate that alongside established NPQ effectors, LHL4 plays a key role in photoprotection, preventing singlet oxygen accumulation in PSII and promoting cell survival upon light stress. LHL4 protective function is distinct from that of NPQ-related proteins, as it specifically and uniquely binds to the transient monomeric form of the core PSII complex, safeguarding its integrity. LHL4 characterization expands our understanding of the interplay between light harvesting and photoprotection mechanisms upon light stress in photosynthetic microalgae.

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“…In parallel, the newly synthesized D1 precursor interacts with PsbI that has already been produced. PsbI-D1 (D1 mod ) is then combined with the D2-Cyt b 559 complex to form the reaction center (RCII) (Dobakova et al, 2007; Zhao et al, 2023). This is followed by proteolytic processing of the D1 precursor at its C-terminus (Anbudurai et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Complexome profiling of the Chlamydomonaspsb28mutant reveals THYLAKOID ENRICHED FRACTION 5 as an early photosystem II assembly factor

Lang,

König,

Venn

et al. 2024

Preprint

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Several auxiliary factors are required for the assembly of photosystem (PS) II, one of which is Psb28. While the absence of Psb28 in cyanobacteria has little effect on PSII assembly, we show here that the Chlamydomonaspsb28-null mutant is severely impaired in PSII assembly, showing drastically reduced PSII supercomplexes, dimers and monomers, while overaccumulating RCII, CP43modand D1mod. The mutant had less PSI and more Cytb6fand showed fewer thylakoid stacks and distorted chloroplast morphology. Complexome profiling of thepsb28mutant revealed that TEF5, the homolog of Arabidopsis PSB33/LIL8, co-migrated particularly with RCII. TEF5 also interacted with PSI. A Chlamydomonastef5null mutant is also severely impaired in PSII assembly and overaccumulates RCII and CP43mod. RC47 was not detectable in the light-growntef5mutant. Our data suggest a possible role for TEF5 in facilitating the assembly of CP47modinto RCII. Both thepsb28andtef5mutants exhibited decreased synthesis of CP47 and PsbH, suggesting negative feedback regulation possibly exerted by the accumulation of RCII and/or CP43modin both mutants. The strong effects of missing auxiliary factors on PSII assembly in Chlamydomonas suggest a more effective protein quality control system in this alga than in land plants and cyanobacteria.One-sentence summaryThe Chlamydomonas psb28 mutant is severely impaired in PSII assembly which via complexome profiling allowed identifying TEF5 as a novel PSII assembly factor that likely facilitates CP47 assembly.The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (https://academic.oup.com/plcell/pages/General-Instructions) is: Michael Schroda (m.schroda@rptu.de).

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The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis

Cited by 4 publications

References 65 publications

Localization of Proteins Involved in the Biogenesis of the Photosynthetic Apparatus to Thylakoid Subdomains in Arabidopsis

Localization of Proteins Involved in the Biogenesis of the Photosynthetic Apparatus to Thylakoid Subdomains in Arabidopsis

Photoreceptor-induced LHL4 protects photosystem II inChlamydomonas reinhardtii

Complexome profiling of the Chlamydomonaspsb28mutant reveals THYLAKOID ENRICHED FRACTION 5 as an early photosystem II assembly factor

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