Organisation of Photosystem I and Photosystem II in red alga Cyanidium caldarium: Encounter of cyanobacterial and higher plant concepts

Gardian, Zdenko; Bumba, Ladislav; Schröfel, Adam; Herbstová, Miroslava; Nebesářová, Jana; Vacha, František

doi:10.1016/j.bbabio.2007.01.021

Cited by 58 publications

(60 citation statements)

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“…The location of PsbQЈ revealed in the present study is consistent with the site suggested from single particle electron microscopic analysis of PSII from another red alga, C. merolae (43), although a previous microscopic analysis suggested a possibly different location of the PsbQЈ in the red alga at a lower resolution (42). Very recently, however, Liu et al (44) reported that cyano-PsbQ was located in the middle of the PSII dimer between two PsbO subunits from two monomers in the lumenal surface of cyanobacterial PSII and interacts with CP47 instead of CP43, based on the cross-linking of a PsbQ dimer and subsequent mass spectrometric analysis.…”

Section: Discussionsupporting

confidence: 90%

“…Red alga is the most primitive eukaryotic algae with their photosynthetic systems resemble in part the prokaryotic cyanobacteria and in part the eukaryotic algae, because the PSII of red algae is associated by phycobilisomes as light-harvesting antenna pigments, whereas its photosystem I binds light-harvesting complex I similar to those found in green algae and higher plant photosystem I (42). So far the structure of PSII has been solved from cyanobacteria at an atomic resolution (5, 6), whereas no crystal structure of eukaryotic PSII has been reported.…”

Section: Discussionmentioning

confidence: 99%

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Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga

Ago

Adachi

Umena

et al. 2016

Journal of Biological Chemistry

111

103

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Photosystem II (PSII) catalyzes light-induced water splitting, leading to the evolution of molecular oxygen indispensible for life on the earth. The crystal structure of PSII from cyanobacteria has been solved at an atomic level, but the structure of eukaryotic PSII has not been analyzed. Because eukaryotic PSII possesses additional subunits not found in cyanobacterial PSII, it is important to solve the structure of eukaryotic PSII to elucidate their detailed functions, as well as evolutionary relationships. Here we report the structure of PSII from a red alga Cyanidium caldarium at 2.76 Å resolution, which revealed the structure and interaction sites of PsbQ, a unique, fourth extrinsic protein required for stabilizing the oxygen-evolving complex in the lumenal surface of PSII. The PsbQ subunit was found to be located underneath CP43 in the vicinity of PsbV, and its structure is characterized by a bundle of four up-down helices arranged in a similar way to those of cyanobacterial and higher plant PsbQ, although helices I and II of PsbQ were kinked relative to its higher plant counterpart because of its interactions with CP43. Furthermore, two novel transmembrane helices were found in the red algal PSII that are not present in cyanobacterial PSII; one of these helices may correspond to PsbW found only in eukaryotic PSII. The present results represent the first crystal structure of PSII from eukaryotic oxygenic organisms, which were discussed in comparison with the structure of cyanobacterial PSII.Oxygenic photosynthesis provides us with food, oxygen, and fuel and is therefore vital to life on the earth. The first reaction occurring in oxygenic photosynthesis is the splitting of water into electrons, protons, and molecular oxygen, among which electrons and protons are utilized for the synthesis of NADPH and ATP, whereas oxygen is supplied to the atmosphere for maintaining aerobic life forms. The water splitting reaction is catalyzed by photosystem II (PSII), 5 an extremely large membrane-protein complex located in thylakoid membranes from prokaryotic cyanobacteria to higher plants. In the case of cyanobacteria, the crystal structure of PSII has been solved with its resolution gradually increased to an atomic level of 1.9 Å (1-6), which showed that PSII contains 17 transmembrane subunits and 3 peripheral, hydrophilic subunits with a total molecular mass of 700 kDa for a dimer.The first oxygenic photosynthetic organism is believed to be the ancestor of cyanobacteria some 2.7 billion years ago (7). Although the subunit compositions of PSII from cyanobacteria to higher plants we see today are rather conserved, some apparent differences exist in both the transmembrane and peripheral subunits among cyanobacteria, various algae, and higher plants (8). One of the remarkable differences is found in the composition and function of extrinsic proteins associated in the lumenal side and required for maintaining the optimal function of the water-splitting reaction. In cyanobacteria, three extrinsic proteins of PsbO (33 kDa), Ps...

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga

Ago

Adachi

Umena

et al. 2016

Journal of Biological Chemistry

111

103

View full text Add to dashboard Cite

show abstract

“…As an evolutionary intermediate between the photosynthetic apparatus of prokaryotic cyanobacteria and that of the eukaryotes in the green lineage, it contains a mixture of prokaryotic and eukaryotic structural traits. Whereas red algal photosystem I (PSI) resembles a higher plant complex, with an crescent-shaped Chla-binding light-harvesting antenna system asymmetrically bound on one side of the core complex (22)(23), PSII of red algae is structurally similar to the cyanobacterial counterpart in that it contains light-harvesting antenna composed of phycobilisomes, large peripheral membrane complexes formed by phycobiliproteins, instead of Chla/ b-binding antenna proteins that constitute the light-harvesting system of green algae and higher plants.…”

Section: Photosystem II (Psii)mentioning

confidence: 99%

A Reaction Center-dependent Photoprotection Mechanism in a Highly Robust Photosystem II from an Extremophilic Red Alga, Cyanidioschyzon merolae

Krupnik

Kotabová

Bezouwen

et al. 2013

Journal of Biological Chemistry

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Background: PSII is a protein complex that captures sunlight to drive water oxidation. Results: Cyanidioschyzon merolae PSII is protected by reversible reaction center-based non-photochemical quenching. Conclusion: C. merolae PSII employs reaction center non-photochemical quenching as the main photoprotective mechanism. Significance: We provide the first direct evidence of the PSII reaction center as the primary locus of non-photochemical quenching in the extremophilic red algae.

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“…Although there have been reports of trimeric forms of PSI in plants (Heinemeyer et al, 2004;Kouril et al, 2005), it is now widely accepted that plant PSI forms only monomeric complexes (Kitmitto et al, 1998;Kouril et al, 2005). Furthermore, it is known that PSI is a monomer in green and red algae (Gardian et al, 2007) as well as in diatoms (Veith and Büchel, 2007).…”

Section: Introductionmentioning

confidence: 99%

Characterization and Evolution of Tetrameric Photosystem I from the Thermophilic Cyanobacterium Chroococcidiopsis sp TS-821

Semchonok

Boekema

et al. 2014

Plant Cell

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ORCID ID: 0000-0002-4045-9815 (B.D.B.)Photosystem I (PSI) is a reaction center associated with oxygenic photosynthesis. Unlike the monomeric reaction centers in green and purple bacteria, PSI forms trimeric complexes in most cyanobacteria with a 3-fold rotational symmetry that is primarily stabilized via adjacent PsaL subunits; however, in plants/algae, PSI is monomeric. In this study, we discovered a tetrameric form of PSI in the thermophilic cyanobacterium Chroococcidiopsis sp TS-821 (TS-821). In TS-821, PSI forms tetrameric and dimeric species. We investigated these species by Blue Native PAGE, Suc density gradient centrifugation, 77K fluorescence, circular dichroism, and single-particle analysis. Transmission electron microscopy analysis of native membranes confirms the presence of the tetrameric PSI structure prior to detergent solubilization. To investigate why TS-821 forms tetramers instead of trimers, we cloned and analyzed its psaL gene. Interestingly, this gene product contains a short insert between the second and third predicted transmembrane helices. Phylogenetic analysis based on PsaL protein sequences shows that TS-821 is closely related to heterocyst-forming cyanobacteria, some of which also have a tetrameric form of PSI. These results are discussed in light of chloroplast evolution, and we propose that PSI evolved stepwise from a trimeric form to tetrameric oligomer en route to becoming monomeric in plants/algae.

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Organisation of Photosystem I and Photosystem II in red alga Cyanidium caldarium: Encounter of cyanobacterial and higher plant concepts

Cited by 58 publications

References 45 publications

Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga

Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga

A Reaction Center-dependent Photoprotection Mechanism in a Highly Robust Photosystem II from an Extremophilic Red Alga, Cyanidioschyzon merolae

Characterization and Evolution of Tetrameric Photosystem I from the Thermophilic Cyanobacterium Chroococcidiopsis sp TS-821

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