Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution

Wei, Xuepeng; Su, Xiaodong; Cao, Peng; Liu, Xiuying; Chang, Wenrui; Li, Mei; Zhang, Xinzheng; Liu, Zhongfan

doi:10.1038/nature18020

Cited by 522 publications

(646 citation statements)

References 67 publications

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“…1D), although it only appeared as a very faint band, suggesting that it is present in substoichiometric amounts in the preparation. As for the ␣-DDM preparations of Arabidopsis analyzed by negative staining EM (12) and the same kind of preparation on spinach analyzed by cryo-EM (25), despite the presence of PsbS, we were not able to find a density corresponding to PsbS in negative-staining EM single particle analysis (supplemental Fig. S1).…”

Section: Resultsmentioning

confidence: 86%

“…Very recently, the near atomic resolution of the spinach C 2 S 2 supercomplex has been solved by using a cryo-EM approach (25). The protocol used for spinach PSII preparation by Wei et al (25) is the one that we previously published for obtaining homogeneous preparations of Arabidopsis PSII supercomplexes with different antenna sizes (12).…”

Section: Photosystem II (Psii)mentioning

confidence: 99%

“…Because measurements on these samples could be performed only in cold conditions and on fresh non-concentrated samples, these were limited to negative staining EM (12) and time-resolved fluorescence spectroscopy (26). However, the smaller C 2 S 2 supercomplex, containing the two strongly bound S-LHCII trimers, but lacking the moderately bound M-LHCII trimers and the monomeric CP24 antenna, was stable enough for its structural determination by single particle cryo-EM (25). In this work we present an improved protocol to obtain similar preparations as described previously (12), but with largely improved stability, thus allowing the use of these preparations for several different experiments that require room temperature conditions and/or at high protein concentration (up to ϳ6 mg/ml, or A cm ϳ80).…”

Section: Photosystem II (Psii)mentioning

confidence: 99%

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Biochemical and Spectroscopic Characterization of Highly Stable Photosystem II Supercomplexes from Arabidopsis

Crepin

Santabarbara

Caffarri

2016

Journal of Biological Chemistry

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Photosystem II (PSII) is a large membrane supercomplex involved in the first step of oxygenic photosynthesis. It is organized as a dimer, with each monomer consisting of more than 20 subunits as well as several cofactors, including chlorophyll and carotenoid pigments, lipids, and ions. The isolation of stable and homogeneous PSII supercomplexes from plants has been a hindrance for their deep structural and functional characterization. In recent years, purification of complexes with different antenna sizes was achieved with mild detergent solubilization of photosynthetic membranes and fractionation on a sucrose gradient, but these preparations were only stable in the cold for a few hours. In this work, we present an improved protocol to obtain plant PSII supercomplexes that are stable for several hours/days at a wide range of temperatures and can be concentrated without degradation. Biochemical and spectroscopic properties of the purified PSII are presented, as well as a study of the complex solubility in the presence of salts. We also tested the impact of a large panel of detergents on PSII stability and found that very few are able to maintain the integrity of PSII. Such new PSII preparation opens the possibility of performing experiments that require room temperature conditions and/or high protein concentrations, and thus it will allow more detailed investigations into the structure and molecular mechanisms that underlie plant PSII function. Photosystem II (PSII)2 is the first complex involved in oxygenic photosynthesis. By using light energy, PSII is capable of extracting electrons from water and starting an electron transport chain that finally reduces carbon into organic matter through the Calvin-Benson cycle. This process sustains the vast majority of life on earth and produces the molecular O 2 necessary for aerobic metabolism.PSII is a large membrane supercomplex composed of several protein subunits and cofactors (chlorophylls and carotenoid pigments, lipids, and ions). The supercomplex is organized in a dimeric form, with each monomer consisting of more than 20 subunits organized in two moieties: the core complex and the antenna system. The core complex is the only part well conserved among all oxygenic photosynthetic organisms (1). Conversely, the antenna systems are very different, being composed of integral membrane proteins in eukaryotes and peripheral proteins (phycobilisomes) in cyanobacteria (2). Significant differences in the organization of the antenna system can also be found in different eukaryotes as a result of different evolutionary pressures.The core complex is composed of several subunits as follows: (i) D1 and D2, which contain the reaction center P680 and the cofactors of the electron transport chain; (ii) CP47 and CP43, which act as inner antennas by coordinating most of the core chlorophyll a molecules (Chls a), and (iii) several low molecular mass subunits, whose roles for the most part are only little understood (3, 4). Most of the differences between eukaryote and prokaryote core ...

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Section: Resultsmentioning

confidence: 86%

Section: Photosystem II (Psii)mentioning

confidence: 99%

Section: Photosystem II (Psii)mentioning

confidence: 99%

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Biochemical and Spectroscopic Characterization of Highly Stable Photosystem II Supercomplexes from Arabidopsis

Crepin

Santabarbara

Caffarri

2016

Journal of Biological Chemistry

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“…Respiration was presumed to be the primary net ATP production source for protein synthesis, and its value is based on experimental data from the Arabidopsis rosette. Lambreva et al, 2014;Wei et al, 2016).Cyanobacterial PetD forms the p-side of the cytochrome b 6 f complex, which accepts protons from plastosemiquinone and defines a route for H + transfer in the complex (Hasan et al, 2013). Also, the transcripts for D1 and PetD proteins are both found to be upregulated in the adg1-1 tpt-2 double mutant, which shows rapid photoinhibition under high light (Schmitz et al, 2014).…”

Section: Protein Stability and The Correlations With Protein Functionmentioning

confidence: 99%

Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

et al. 2017

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We applied 15 N labeling approaches to leaves of the Arabidopsis thaliana rosette to characterize their protein degradation rate and understand its determinants. The progressive labeling of new peptides with 15 N and measuring the decrease in the abundance of >60,000 existing peptides over time allowed us to define the degradation rate of 1228 proteins in vivo. We show that Arabidopsis protein half-lives vary from several hours to several months based on the exponential constant of the decay rate for each protein. This rate was calculated from the relative isotope abundance of each peptide and the fold change in protein abundance during growth. Protein complex membership and specific protein domains were found to be strong predictors of degradation rate, while N-end amino acid, hydrophobicity, or aggregation propensity of proteins were not. We discovered rapidly degrading subunits in a variety of protein complexes in plastids and identified the set of plant proteins whose degradation rate changed in different leaves of the rosette and correlated with leaf growth rate. From this information, we have calculated the protein turnover energy costs in different leaves and their key determinants within the proteome.

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“…Current high-resolution structures of thermophilic cyanobacterial PSII (3,4), and lower resolution structures of the red algal (5) and higher plant photosystems (6), have been critically important in furthering our understanding of the molecular organization of PSII. Structurally, the PSII reaction center core is composed of five proteins: D1, D2, the α-and β-subunits of cytochrome b 559 , and PsbI.…”

mentioning

confidence: 99%

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Kale

Hebert

Frankel

et al. 2017

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

134

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The Photosystem II reaction center is vulnerable to photoinhibition. The D1 and D2 proteins, lying at the core of the photosystem, are susceptible to oxidative modification by reactive oxygen species that are formed by the photosystem during illumination. Using spin probes and EPR spectroscopy, we have determined that both O 2 . The identification of specific amino acid residues oxidized by reactive oxygen species provides insights into the mechanism of damage to the D1 and D2 proteins under light stress.photosynthesis | Photosystem II | reactive oxygen species | photo inhibition | mass spectrometry P hotosystem II (PSII) functions as a water-plastoquinone oxidoreductase (1, 2) and is a thylakoid membrane pigmentprotein complex present in all oxygenic photosynthetic organisms (cyanobacteria, algae, and higher plants). Current high-resolution structures of thermophilic cyanobacterial PSII (3, 4), and lower resolution structures of the red algal (5) and higher plant photosystems (6), have been critically important in furthering our understanding of the molecular organization of PSII. Structurally, the PSII reaction center core is composed of five proteins: D1, D2, the α-and β-subunits of cytochrome b 559 , and PsbI. These components bind all of the redox-active cofactors of PSII.Excitation energy transfer and electron transport within PSII are unavoidably associated with production of reactive oxygen species (ROS) when the absorption of light by the chlorophyll antenna exceeds the capacity for energy utilization. Many mechanisms for ROS production have been proposed (for reviews, see refs. 7 and 8). Briefly, singlet oxygen ( 1 O 2 ) may be formed by excitation energy transfer from triplet chlorophylls (formed either by the change in orientation of the spin of an excited electron in the PSII antenna complex, or via charge recombination of the primary radical pair 3 [P 680 •+ Pheo •− ]) to O 2 (9, 10). ROS production by electron transport involves either the two-electron oxidation of water or the one-electron reduction of O 2 on the PSII electron donor and acceptor sides, respectively. On the PSII electron donor side, a twoelectron oxidation of water leads to the formation of hydrogen peroxide (H 2 O 2 ), which may be oxidized to the superoxide anion radical (O 2•−

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Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution

Cited by 522 publications

References 67 publications

Biochemical and Spectroscopic Characterization of Highly Stable Photosystem II Supercomplexes from Arabidopsis

Biochemical and Spectroscopic Characterization of Highly Stable Photosystem II Supercomplexes from Arabidopsis

Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

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