Rubredoxin 1 promotes the proper folding of D1 and is not required for heme b559 assembly in Chlamydomonas photosystem II

Calderon, Robert H.; Vitry, Catherine de; Wollman, Françis-André; Niyogi, Krishna

doi:10.1016/j.jbc.2023.102968

Cited by 14 publications

(9 citation statements)

References 63 publications

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“…PsbY shows no sequence relation to the protein Psb1 identified in this study ( Kawakami et al., 2009 ; PDB 3A0B). The pre-PSII-1 assembly intermediate does not contain LPA2 or rubredoxin, which might function in catalytic capacities ( García-Cerdán et al., 2019 ; Cecchin et al., 2021 ; Spaniol et al., 2022 ; Calderon et al., 2023 ).…”

Section: Resultsmentioning

confidence: 99%

Structure of native photosystem II assembly intermediate from Chlamydomonas reinhardtii

Fadeeva,

Klaiman,

Kandiah

et al. 2024

Front. Plant Sci.

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Chlamydomonas reinhardtii Photosystem II (PSII) is a dimer consisting of at least 13 nuclear-encoded and four chloroplast-encoded protein subunits that collectively function as a sunlight-driven oxidoreductase. In this study, we present the inaugural structure of a green alga PSII assembly intermediate (pre-PSII-int). This intermediate was isolated from chloroplast membranes of the temperature-sensitive mutant TSP4, cultivated for 14 hours at a non-permissive temperature. The assembly state comprises a monomer containing subunits A, B, C, D, E, F, H, I, K, and two novel assembly factors, Psb1 and Psb2. Psb1 is identified as a novel transmembrane helix located adjacent to PsbE and PsbF (cytochrome b559). The absence of PsbJ, typically found in mature PSII close to this position, indicates that Psb1 functions as an assembly factor. Psb2 is an eukaryotic homolog of the cyanobacterial assembly factor Psb27. The presence of iron, coupled with the absence of QA, QB, and the manganese cluster, implies a protective mechanism against photodamage and provides insights into the intricate assembly process.

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Section: Resultsmentioning

confidence: 99%

Structure of native photosystem II assembly intermediate from Chlamydomonas reinhardtii

Fadeeva,

Klaiman,

Kandiah

et al. 2024

Front. Plant Sci.

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“…Since the accumulation of ATP synthase in atpG‐kd ( E236 ) is limited by the amount of ATPG subunit, we wondered whether the other subunits possibly produced in excess were subsequently removed by proteolysis. One candidate for such proteolytic disposal is the thylakoid FTSH protease, a transmembrane FTSH1‐FTSH2 hetero‐hexamer, which degrades damaged subunit D1 during PSII repair cycle, cytochrome b 6 f subunits and thylakoid membrane proteins involved in cytochrome b 6 f biogenesis upon nutrient starvation or in cytochrome b 6 f mutants, and LHCI antenna proteins in chlorophyll b ‐less mutants (Bujaldon et al., 2017; Calderon et al., 2023; De Mia et al., 2019; Kato et al., 2023; Malnoë et al., 2011, 2014; Schroda & de Vitry, 2022; Wei et al., 2014). We thus crossed the atpG and atpF mutants to the proteolytic‐defective ftsh1‐1 mutant (Malnoë et al., 2014).…”

Section: Resultsmentioning

confidence: 99%

Chloroplast ATP synthase biogenesis requires peripheral stalk subunits AtpF and ATPG and stabilization of atpE mRNA by OPR protein MDE1

Chaux,

Jarrige,

Rodrigues‐Azevedo

et al. 2023

The Plant Journal

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SUMMARYChloroplast ATP synthase contains subunits of plastid and nuclear genetic origin. To investigate the coordinated biogenesis of this complex, we isolated novel ATP synthase mutants in the green alga Chlamydomonas reinhardtii by screening for high light sensitivity. We report here the characterization of mutants affecting the two peripheral stalk subunits b and b′, encoded respectively by the atpF and ATPG genes, and of three independent mutants which identify the nuclear factor MDE1, required to stabilize the chloroplast‐encoded atpE mRNA. Whole‐genome sequencing revealed a transposon insertion in the 3′UTR of ATPG while mass spectrometry shows a small accumulation of functional ATP synthase in this knock‐down ATPG mutant. In contrast, knock‐out ATPG mutants, obtained by CRISPR‐Cas9 gene editing, fully prevent ATP synthase function and accumulation, as also observed in an atpF frame‐shift mutant. Crossing ATP synthase mutants with the ftsh1‐1 mutant of the major thylakoid protease identifies AtpH as an FTSH substrate, and shows that FTSH significantly contributes to the concerted accumulation of ATP synthase subunits. In mde1 mutants, the absence of atpE transcript fully prevents ATP synthase biogenesis and photosynthesis. Using chimeric atpE genes to rescue atpE transcript accumulation, we demonstrate that MDE1, a novel octotricopeptide repeat (OPR) protein, genetically targets the atpE 5′UTR. In the perspective of the primary endosymbiosis (~1.5 Gy), the recruitment of MDE1 to its atpE target exemplifies a nucleus/chloroplast interplay that evolved rather recently, in the ancestor of the CS clade of Chlorophyceae, ~300 My ago.

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“…In Chlamydomonas , One-Helix Protein 2 (OHP2) stabilizes D1 during its translation by promoting chlorophyll association [ 109 ]. Another assembly factor, RBD1, promotes D1 stabilization [ 110 , 111 ] and is also involved in the delivery and/or reduction of the non-heme iron ion near the stromal surface of PSII [ 112 ]. Next, CP47 is translated and binds to create the RC47 complex.…”

Section: Discussionmentioning

confidence: 99%

Assembly and Repair of Photosystem II in Chlamydomonas reinhardtii

Mehra,

Wang,

Russell

et al. 2024

Plants

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Oxygenic photosynthetic organisms use Photosystem II (PSII) to oxidize water and reduce plastoquinone. Here, we review the mechanisms by which PSII is assembled and turned over in the model green alga Chlamydomonas reinhardtii. This species has been used to make key discoveries in PSII research due to its metabolic flexibility and amenability to genetic approaches. PSII subunits originate from both nuclear and chloroplastic gene products in Chlamydomonas. Nuclear-encoded PSII subunits are transported into the chloroplast and chloroplast-encoded PSII subunits are translated by a coordinated mechanism. Active PSII dimers are built from discrete reaction center complexes in a process facilitated by assembly factors. The phosphorylation of core subunits affects supercomplex formation and localization within the thylakoid network. Proteolysis primarily targets the D1 subunit, which when replaced, allows PSII to be reactivated and completes a repair cycle. While PSII has been extensively studied using Chlamydomonas as a model species, important questions remain about its assembly and repair which are presented here.

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Rubredoxin 1 promotes the proper folding of D1 and is not required for heme b559 assembly in Chlamydomonas photosystem II

Cited by 14 publications

References 63 publications

Structure of native photosystem II assembly intermediate from Chlamydomonas reinhardtii

Structure of native photosystem II assembly intermediate from Chlamydomonas reinhardtii

Chloroplast ATP synthase biogenesis requires peripheral stalk subunits AtpF and ATPG and stabilization of atpE mRNA by OPR protein MDE1

Assembly and Repair of Photosystem II in Chlamydomonas reinhardtii

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