Synthesis and assembly of thylakoid protein complexes: multiple assembly steps of photosystem II

Rokka, Anne; Suorsa, Marjaana; Saleem, Ammar; Battchikova, Natalia; Aro, Eva‐Mari

doi:10.1042/bj20042098

Cited by 171 publications

(139 citation statements)

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“…Immunoblots were quantified with FluorChem Image Analyzer (Alpha Innotech Corp.). Blue native gel electrophoresis was performed as described earlier (25).…”

Section: Plant Materials and Growth Conditions-arabidopsis Thalianamentioning

confidence: 99%

PsbR, a Missing Link in the Assembly of the Oxygen-evolving Complex of Plant Photosystem II

Suorsa

Sirpiö

Allahverdiyeva

et al. 2006

Journal of Biological Chemistry

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123

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The oxygen-evolving complex of eukaryotic photosystem II (PSII) consists of three extrinsic nuclear-encoded subunits, PsbO (33 kDa), PsbP (23 kDa), and PsbQ (17 kDa). Additionally, the 10-kDa PsbR protein has been found in plant PSII and anticipated to play a role in water oxidation, yet the physiological significance of PsbR has remained obscure. Using the Arabidopsis psbR mutant, we showed that the light-saturated rate of oxygen evolution is strongly reduced in the absence of PsbR, particularly in low light-grown plants. Lack of PsbR also induced a reduction in the content of both the PsbP and the PsbQ proteins, and a near depletion of these proteins was observed under steady state low light conditions. This regulation occurred post-transcriptionally and likely involves a proteolytic degradation of the PsbP and PsbQ proteins in the absence of an assembly partner, proposed to be the PsbR protein. Stable assembly of PsbR in the PSII core complex was, in turn, shown to require a chloroplast-encoded intrinsic low molecular mass PSII subunit PsbJ. Our results provided evidence that PsbR is an important link in the PSII core complex for stable assembly of the oxygen-evolving complex protein PsbP, whereas the effects on the assembly of PsbQ are probably indirect. The physiological role of the PsbR, PsbP, and PsbQ proteins is discussed in light of their peculiar expression in response to growth light conditions.

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“…Immunoblots were quantified with FluorChem Image Analyzer (Alpha Innotech Corp.). Blue native gel electrophoresis was performed as described earlier (25).…”

Section: Plant Materials and Growth Conditions-arabidopsis Thalianamentioning

confidence: 99%

PsbR, a Missing Link in the Assembly of the Oxygen-evolving Complex of Plant Photosystem II

Suorsa

Sirpiö

Allahverdiyeva

et al. 2006

Journal of Biological Chemistry

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123

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“…Binding of pre-CP47 to the RC forms the RC47 (CP43-less monomer). Concomitant attachment of pre-CP43 leads to the assembly of the PSII monomer and enables attachment of the oxygen-evolving complex (Rokka et al, 2005;Boehm et al, 2012;Komenda et al, 2012;Nickelsen and Rengstl, 2013). Following dimerization of the monomer, the outer chlorophyll a/b binding antenna proteins CP29, CP26, and CP24 and finally trimeric light-harvesting complex II (LHCII) proteins are attached to form the PSII supercomplexes (Kouril et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

“…The nuclear-encoded low molecular weight PsbW protein has been shown to be important in this process in plants ( García-Cerdán et al, 2011). The precise sequential attachment of other low molecular weight subunits is still under debate (Rokka et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

PsbN Is Required for Assembly of the Photosystem II Reaction Center in Nicotiana tabacum

et al. 2014

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ORCID ID: 0000-0003-2973-9514 (J.M.)The chloroplast-encoded low molecular weight protein PsbN is annotated as a photosystem II (PSII) subunit. To elucidate the localization and function of PsbN, encoded on the opposite strand to the psbB gene cluster, we raised antibodies and inserted a resistance cassette into PsbN in both directions. Both homoplastomic tobacco (Nicotiana tabacum) mutants ΔpsbN-F and ΔpsbN-R show essentially the same PSII deficiencies. The mutants are extremely light sensitive and failed to recover from photoinhibition. Although synthesis of PSII proteins was not altered significantly, both mutants accumulated only ;25% of PSII proteins compared with the wild type. Assembly of PSII precomplexes occurred at normal rates, but heterodimeric PSII reaction centers (RCs) and higher order PSII assemblies were not formed efficiently in the mutants. The ΔpsbN-R mutant was complemented by allotopic expression of the PsbN gene fused to the sequence of a chloroplast transit peptide in the nuclear genome. PsbN represents a bitopic trans-membrane peptide localized in stroma lamellae with its highly conserved C terminus exposed to the stroma. Significant amounts of PsbN were already present in dark-grown seedling. Our data prove that PsbN is not a constituent subunit of PSII but is required for repair from photoinhibition and efficient assembly of the PSII RC.

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“…Harmful photosynthetic side reactions cannot be avoided completely and become a serious problem under stress (e.g., high light stress). The main target of photoinhibition (PI) is the D1 subunit of the water-splitting photosystem II (PSII) (1,2). The D1 subunit is buried in the massive (1,400 kDa) PSII holocomplex that is organized as a dimer and binds between two and four trimeric light-harvesting complex IIs (LHCIIs) (3,4).…”

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confidence: 99%

Architectural switch in plant photosynthetic membranes induced by light stress

Herbstová

Tietz

Kinzel

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

143

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Unavoidable side reactions of photosynthetic energy conversion can damage the water-splitting photosystem II (PSII) holocomplex embedded in the thylakoid membrane system inside chloroplasts. Plant survival is crucially dependent on an efficient molecular repair of damaged PSII realized by a multistep repair cycle. The PSII repair cycle requires a brisk lateral protein traffic between stacked grana thylakoids and unstacked stroma lamellae that is challenged by the tight stacking and low protein mobility in grana. We demonstrated that high light stress induced two main structural changes that work synergistically to improve the accessibility between damaged PSII in grana and its repair machinery in stroma lamellae: lateral shrinkage of grana diameter and increased protein mobility in grana thylakoids. It follows that high light stress triggers an architectural switch of the thylakoid network that is advantageous for swift protein repair. Studies of the thylakoid kinase mutant stn8 and the double mutant stn7/8 demonstrate the central role of protein phosphorylation for the structural alterations. These findings are based on the elaboration of mathematical tools for analyzing confocal laser-scanning microscopic images to study changes in the sophisticated thylakoid architecture in intact protoplasts.confocal microscopy | macromolecular crowding | photosynthesis P hotosynthetic transformation of sunlight into metabolic energy equivalents is a dangerous venture, because toxic side products of the primary photochemical processes can lead to uncontrolled damage. Harmful photosynthetic side reactions cannot be avoided completely and become a serious problem under stress (e.g., high light stress). The main target of photoinhibition (PI) is the D1 subunit of the water-splitting photosystem II (PSII) (1, 2). The D1 subunit is buried in the massive (1,400 kDa) PSII holocomplex that is organized as a dimer and binds between two and four trimeric light-harvesting complex IIs (LHCIIs) (3, 4). Estimates predict that without repair of damaged PSII, the efficiency for photosynthetic energy conversion would drop below 5% (5). Consequently, plants would not survive in a highly dynamic and competitive natural environment. Plants address this challenge through the evolutionary invention of one of the fastest and most efficient molecular repair mechanisms in nature, the PSII repair cycle (5-7).The PSII repair cycle consist of a series of events, including phosphorylation/ dephosphorylation of PSII subunits, holocomplex disassembly/reassembly, and D1 degradation/de novo synthesis (8-10). All of these reactions are harbored in or at the thylakoid membrane system inside the chloroplast. The complex folding of the thylakoid membrane leads to a structural differentiation into stacked grana regions interconnected by unstacked stroma lamellae (11)(12)(13). This structural heterogeneity is accompanied by, and partly driven by, differential protein distributions. PSII and LHCII are concentrated in grana stacks, photosystem I (PSI) and the ATPas...

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Synthesis and assembly of thylakoid protein complexes: multiple assembly steps of photosystem II

Cited by 171 publications

References 56 publications

PsbR, a Missing Link in the Assembly of the Oxygen-evolving Complex of Plant Photosystem II

PsbR, a Missing Link in the Assembly of the Oxygen-evolving Complex of Plant Photosystem II

PsbN Is Required for Assembly of the Photosystem II Reaction Center in Nicotiana tabacum

Architectural switch in plant photosynthetic membranes induced by light stress

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