Protein Of Photosystem Research Articles

Insights into the Photoprotective Switch of the Major Light-harvesting Complex II (LHCII): A PRESERVED CORE OF ARGININE-GLUTAMATE INTERLOCKED HELICES COMPLEMENTED BY ADJUSTABLE LOOPS

Light-harvesting antennae of the LHC family form transmembrane three-helix bundles of which two helices are interlocked by conserved arginine-glutamate (Arg-Glu) ion pairs that form ligation sites for chlorophylls. The antenna proteins of photosystem II have an intriguing dual function. In excess light, they can switch their conformation from a light-harvesting into a photoprotective state, in which the excess and harmful excitation energies are safely dissipated as heat. Here we applied magic angle spinning NMR and selective Arg isotope enrichment as a noninvasive method to analyze the Arg structures of the major light-harvesting complex II (LHCII). The conformations of the Arg residues that interlock helix A and B appear to be preserved in the light-harvesting and photoprotective state. Several Arg residues have very downfield-shifted proton NMR responses, indicating that they stabilize the complex by strong hydrogen bonds. For the Arg Cα chemical shifts, differences are observed between LHCII in the active, light-harvesting and in the photoprotective, quenched state. These differences are attributed to a conformational change of the Arg residue in the stromal loop region. We conclude that the interlocked helices of LHCII form a rigid core. Consequently, the LHCII conformational switch does not involve changes in A/B helix tilting but likely involves rearrangements of the loops and helical segments close to the stromal and lumenal ends.

Inactivation of sll0136 gene in Synechocystis sp. PCC 6803 results in the disturbance in protein biogenesis of photosynthetic complexes

The genome of cyanobacterium Synechocystis sp. PCC 6803 contains the sll0136 (pepP) gene encoding the putative homolog of proline aminopeptidase PII (AMPPII) of the heterotrophic bacterium Escherichia coli. AMPPII is known to cleave the N-terminal amino acid residue of peptides and proteins only in the case of a penultimate proline position. The Synechocystis sp. PCC 6803 insertion mutant with inactivated pepP gene is characterized by the reduced content of phycobiliproteins and also proteins of photosystem II, which may be related to the reduced synthesis or stability of corresponding proteins. A possible involvement of PepP in biogenesis of proteins of the photosynthetic apparatus is discussed.

Transcript patterns of chloroplast-encoded genes in cultured Symbiodinium spp. (Dinophyceae): testing the influence of a light shift and diel periodicity.

Microalgae possess numerous cellular mechanisms specifically employed for acclimating the photosynthetic pathways to changes in the physical environment. Despite the importance of coral-dinoflagellate symbioses, little focus has been given as to how the symbiotic algae (Symbiodinium spp.) regulate the expression of their photosynthetic genes. This study used real-time PCR to investigate the transcript abundance of the plastid-encoded genes, psbA (encoding the D1 protein of photosystem II) and psaA (encoding the P700 protein in photosystem I), within the cultured Symbiodinium ITS-2 (internal transcribed spacer region) types A20 and A13. Transcript abundance was monitored during a low to high-light shift, as well as over a full diel light cycle. In addition, psaA was characterized in three isolates (A20, A13, and D4-5) and noted as another example of a dinoflagellate plastid gene encoded on a minicircle. In general, the overall incongruence of transcript patterns for both psbA and psaA between the Symbiodinium isolates and other models of transcriptionally controlled chloroplast gene expression (e.g., Pisum sativum [pea], Sinapis alba [mustard seedling], and Synechocystis sp. PCC 6803 [cyanobacteria]) suggests that Symbiodinium is reliant on posttranscriptional mechanisms for homeostatic regulation of its photosynthetic proteins.

Spectroscopic Study of the Light-Harvesting CP29 Antenna Complex of Photosystem II—Part I

Recent structural data revealed that the CP29 protein of higher plant photosystem II (PSII) contains 13 chlorophylls (Chl's) per complex (Pan et al. Nat. Struct. Mol. Biol. 2011, 18, 309), i.e., five Chl's more than in the predicted CP29 homology-based structure model (Bassi et al. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 10056). This lack of consensus presents a constraint on the interpretation of CP29 optical spectra and their underlying electronic structure. To address this problem, we present new low-temperature (5 K) absorption, fluorescence, and hole-burned (HB) spectra for CP29 proteins from spinach, which are compared with the previously reported data. We focus on excitation energy transfer (EET) and the nature of the lowest-energy state(s). We argue that CP29 proteins previously studied by HB spectroscopy lacked at least one Chl a molecule (i.e., a615 or a611), which along with Chl a612 contribute to the lowest energy state in more intact CP29, and one Chl b (most likely b607). This is why the low-energy state and fluorescence maxima reported by Pieper et al. (Photochem. Photobiol.2000, 71, 574) were blue-shifted by ~1 nm, the low-energy state appeared to be highly localized on a single Chl a molecule, and the position of the low-energy state was independent of burning fluence. In contrast, the position of the nonresonant HB spectrum shifts blue with increasing fluence in intact CP29, as this state is strongly contributed to by several pigments (i.e., a611, a612, a615, and a610). Zero-phonon hole widths obtained for the Chl b band at 638.5 nm (5 K) revealed two independent Chl b → Chl a EET times, i.e., 4 ± 0.5 and 0.4 ± 0.1 ps. The latter value is a factor of 2 faster than previously observed by HB spectroscopy and very similar to the one observed by Gradinaru et al. (J. Phys. Chem. B 2000, 104, 9330) in pump-probe experiments. EET time from 650 nm Chl b → Chl a and downward EET from Chl(s) a state(s) at 665 nm occurs in 4.9 ± 0.7 ps. These findings provide important constraints for excitonic calculations that are discussed in the accompanying paper (part II, DOI 10.1021/jp4004278 ).

Nucleus-Encoded Light-Harvesting Chlorophyll a/b Proteins are Imported Normally into Chlorophyll b-Free Chloroplasts of Arabidopsis

Chloroplast-located proteins which are encoded by the nuclear genome have to be imported from the cytosol into the organelle in a posttranslational manner. Among these nuclear-encoded chloroplast proteins are the light-harvesting chlorophyll a/b-binding proteins (LHCPs). After translation in the cytosol, precursor proteins of LHCPs are imported via the TOC/TIC translocase, processed to their mature size to insert into thylakoid membranes where they recruit chlorophylls a and b to form pigment-protein complexes. The translocation of proteins is a highly regulated process which employs several regulators. To analyze whether CAO (chlorophyll a oxigenase) which converts chlorophyll a to chlorophyll b at the inner chloroplast membrane, is one of these regulators, we performed import reactions utilizing a homozygous loss-of-function mutant (cao-1). We imported in vitro translated and (35)S-labeled precursor proteins of light-harvesting proteins of photosystem II LHCB1, LHCB4, and LHCB5 into chloroplasts isolated from cao-1 and show that import of precursor proteins and their processing to mature forms are not impaired in the mutant. Therefore, regulation of the import machinery cannot be responsible for the decreased steady-state levels of light-harvesting complex (LHC) proteins. Regulation does not take place at the transcriptional level either, because Lhcb mRNAs are not down-regulated. Additionally, reduced steady-state levels of LHCPs also do not occur due to posttranslational turnover of non-functional LHCPs in chloroplasts. Taken together, our data show that plants in the absence of CAO and therefore devoid of chlorophyll b are not influenced in their import behavior of LHC proteins.

Proteins Involved in Distinct Phases of Cold Hardening Process in Frost Resistant Winter Barley (Hordeum vulgare L.) cv Luxor

Winter barley is an economically important cereal crop grown in higher latitudes and altitudes where low temperatures represent an important environmental constraint limiting crop productivity. In this study changes in proteome of leaves and crowns in a frost tolerant winter barley cv. Luxor in relation to short and long term periods of cold followed by a brief frost treatment were studied in order to disclose proteins responsible for the cold hardening process in distinct plant tissues. The mentioned changes have been monitored using two dimensional difference gel electrophoresis (2D-DIGE) with subsequent peptide-mapping protein identification. Regarding approximately 600–700 distinct protein spots detected on 2D gels, there has been found at least a two-fold change after exposure to low temperatures in about 10% of proteins in leaves and 13% of proteins in crowns. Protein and nitrogen metabolic processes have been influenced by low temperature to a similar extent in both tissues while catabolism, carbohydrate metabolism and proteins involved in stress response have been more affected in crowns than in leaves. The range of changes in protein abundance was generally higher in leaves and chloroplast proteins were frequently affected which suggests a priority to protect photosynthetic apparatus. Overall, our data proved existence of slightly different response strategies to low temperature stress in crowns and leaves, i.e., tissues with different biological role. Moreover, there have been found several proteins with large increase in accumulation, e.g., 33 kDa oxygen evolving protein of photosystem II in leaves and “enhanced disease susceptibility 1” in crowns; these proteins might have potential to indicate an enhanced level of frost tolerance in barley.

Redox Regulation of Thylakoid Protein Kinases and Photosynthetic Gene Expression

Photosynthetic organisms are subjected to frequent changes in their environment that include fluctuations in light quality and quantity, temperature, CO(2) concentration, and nutrient availability. They have evolved complex responses to these changes that allow them to protect themselves against photo-oxidative damage and to optimize their growth under these adverse conditions. In the case of light changes, these acclimatory processes can occur in either the short or the long term and are mainly mediated through the redox state of the plastoquinone pool and the ferredoxin/thioredoxin system. Short-term responses involve a dynamic reorganization of photosynthetic complexes, and long-term responses (LTRs) modulate the chloroplast and nuclear gene expression in such a way that the levels of the photosystems and their antennae are rebalanced for an optimal photosynthetic performance. These changes are mediated through a complex signaling network with several protein kinases and phosphatases that are conserved in land plants and algae. The phosphorylation status of the light-harvesting proteins of photosystem II and its core proteins is mainly determined by two complementary kinase-phosphatase pairs corresponding to STN7/PPH1 and STN8/PBCP, respectively. The activity of the Stt7 kinase is principally regulated by the redox state of the plastoquinone pool, which in turn depends on the light irradiance, ambient CO(2) concentration, and cellular energy status. In addition, this kinase is also involved in the LTR. Other chloroplast kinases modulate the activity of the plastid transcriptional machinery, but the global signaling network that connects all of the identified kinases and phosphatases is still largely unknown.

An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures

To protect the photosynthetic apparatus against photo-damage in high sunlight, the photosynthetic antenna of oxygenic organisms can switch from a light-harvesting to a photoprotective mode through the process of non-photochemical quenching (NPQ). There is growing evidence that light-harvesting proteins of photosystem II participate in photoprotection by a built-in capacity to switch their conformation between light-harvesting and energy-dissipating states. Here we applied high-resolution Magic-Angle Spinning Nuclear Magnetic Resonance on uniformly 13C-enriched major light-harvesting complex II (LHCII) of Chlamydomonas reinhardtii in active or quenched states. Our results reveal that the switch into a dissipative state is accompanied by subtle changes in the chlorophyll (Chl) a ground-state electronic structures that affect their NMR responses, particularly for the macrocycle 13C4, 13C5 and 13C6 carbon atoms. Inspection of the LHCII X-ray structures shows that of the Chl molecules in the terminal emitter domain, where excited-state energy accumulates prior to further transfer or dissipation, the C4, 5 and 6 atoms are in closest proximity to lutein; supporting quenching mechanisms that involve altered Chl–lutein interactions in the dissipative state. In addition the observed changes could represent altered interactions between Chla and neoxanthin, which alters its configuration under NPQ conditions. The Chls appear to have increased dynamics in unquenched, detergent-solubilized LHCII. Our work demonstrates that solid-state Nuclear Magnetic Resonance is applicable to investigate high-resolution structural details of light-harvesting proteins in varied functional conditions, and represents a valuable tool to address their molecular plasticity associated with photoprotection.

Structural, functional and auxiliary proteins of photosystem II

Photosystem II (PSII) is the water-splitting enzyme complex of photosynthesis and consists of a large number of protein subunits. Most of these proteins have been structurally and functionally characterized, although there are differences between PSII of plants, algae and cyanobacteria. Here we catalogue all known PSII proteins giving a brief description, where possible of their genetic origin, physical properties, structural relationships and functions. We have also included details of auxiliary proteins known at present to be involved in the in vivo assembly, maintenance and turnover of PSII and which transiently bind to the reaction centre core complex. Finally, we briefly give details of the proteins which form the outer light-harvesting systems of PSII in different types of organisms.

Reciprocal Regulation of Protein Synthesis and Carbon Metabolism for Thylakoid Membrane Biogenesis

Author SummaryMetabolic control of gene expression coordinates the levels of specific gene products to meet cellular demand for their activities. This control can be exerted by metabolites acting as regulatory signals on a class of metabolic enzymes with dual functions as regulators of gene expression. However, little is known about how metabolic signals affect the balance between enzymatic and regulatory roles of these proteins. Here, we report an example of a protein with dual functions in gene expression and carbon metabolism. The chloroplast pyruvate dehydrogenase complex is well-known to produce activated di-carbon precursors for fatty acid, which is required for lipid synthesis. Our results show that a subunit of this enzyme forms ribonucleoprotein particles and influences chloroplast mRNA translation. Conversely, RNA binding affects pyruvate dehydrogenase (metabolic) activity. These findings offer insight into how intracellular metabolic signaling and gene expression are reciprocally regulated during membrane biogenesis. In addition, our results suggest that these dual roles of the protein might exist in evolutionary distant organisms ranging from cyanobacteria to humans.

Stromal protein degradation is incomplete in Arabidopsis thaliana autophagy mutants undergoing natural senescence

BackgroundDegradation of highly abundant stromal proteins plays an important role in the nitrogen economy of the plant during senescence. Lines of evidence supporting proteolysis within the chloroplast and outside the chloroplast have been reported. Two extra-plastidic degradation pathways, chlorophagy and Rubisco Containing Bodies, rely on cytoplasmic autophagy.ResultsIn this work, levels of three stromal proteins (Rubisco large subunit, chloroplast glutamine synthetase and Rubisco activase) and one thylakoid protein (the major light harvesting complex protein of photosystem II) were measured during natural senescence in WT and in two autophagy T-DNA insertion mutants (atg5 and atg7). Thylakoid-localized protein decreased similarly in all genotypes, but stromal protein degradation was incomplete in the two atg mutants. In addition, degradation of two stromal proteins was observed in chloroplasts isolated from mid-senescence leaves.ConclusionsThese data suggest that autophagy does contribute to the complete proteolysis of stromal proteins, but does not play a major degenerative role. In addition, support for in organello degradation is provided.

Emerging trade‐offs – impact of photoprotectants (PsbS, xanthophylls, and vitamin E) on oxylipins as regulators of development and defense

This review summarizes evidence for a mechanistic link between plant photoprotection and the synthesis of oxylipin hormones as regulators of development and defense. Knockout mutants of Arabidopsis, deficient in various key components of the chloroplast photoprotection system, consistently produced greater concentrations of the hormone jasmonic acid or its precursor 12- oxo-phytodienoic acid (OPDA), both members of the oxylipin messenger family. Characterized plants include several mutants deficient in PsbS (an intrinsic chlorophyll-binding protein of photosystem II) or pigments (zeaxanthin and/or lutein) required for photoprotective thermal dissipation of excess excitation energy in the chloroplast and a mutant deficient in reactive oxygen detoxification via the antioxidant vitamin E (tocopherol). Evidence is also presented that certain plant defenses against herbivores or pathogens are elevated for these mutants. This evidence furthermore indicates that wild-type Arabidopsis plants possess less than maximal defenses against herbivores or pathogens, and suggest that plant lines with superior defenses against abiotic stress may have lower biotic defenses. The implications of this apparent trade-off between abiotic and biotic plant defenses for plant ecology as well as for plant breeding/engineering are explored, and the need for research further addressing this important issue is highlighted.

1P255 FTIR study on the functions of the extrinsic proteins in cyanobacterial photosystem II: Evolutionary aspect of extrinsic proteins(18B. Photobiology: Photosynthesis,Poster)

1P255 FTIR study on the functions of the extrinsic proteins in cyanobacterial photosystem II: Evolutionary aspect of extrinsic proteins(18B. Photobiology: Photosynthesis,Poster)

Transcriptional Response of Two Core Photosystem Genes in Symbiodinium spp. Exposed to Thermal Stress

Mutualistic symbioses between scleractinian corals and endosymbiotic dinoflagellates (Symbiodinium spp.) are the foundation of coral reef ecosystems. For many coral-algal symbioses, prolonged episodes of thermal stress damage the symbiont's photosynthetic capability, resulting in its expulsion from the host. Despite the link between photosynthetic competency and symbiont expulsion, little is known about the effect of thermal stress on the expression of photosystem genes in Symbiodinium. This study used real-time PCR to monitor the transcript abundance of two important photosynthetic reaction center genes, psbA (encoding the D1 protein of photosystem II) and psaA (encoding the P700 protein of photosystem I), in four cultured isolates (representing ITS2-types A13, A20, B1, and F2) and two in hospite Symbiodinium spp. within the coral Pocillopora spp. (ITS2-types C1b-c and D1). Both cultured and in hospite Symbiodinium samples were exposed to elevated temperatures (32°C) over a 7-day period and examined for changes in photochemistry and transcript abundance. Symbiodinium A13 and C1b-c (both thermally sensitive) demonstrated significant declines in both psbA and psaA during the thermal stress treatment, whereas the transcript levels of the other Symbiodinium types remained stable. The downregulation of both core photosystem genes could be the result of several different physiological mechanisms, but may ultimately limit repair rates of photosynthetic proteins, rendering some Symbiodinium spp. especially susceptible to thermal stress.

Balancing photosynthetic electron flow is critical for cyanobacterial acclimation to nitrogen limitation

Nitrogen limitation forces photosynthetic organisms to reallocate available nitrogen to essential functions. At the same time, it increases the probability of photo-damage by limiting the rate of energy-demanding metabolic processes, downstream of the photosynthetic apparatus. Non-diazotrophic cyanobacteria cope with this situation by decreasing the size of their phycobilisome antenna and by modifying their photosynthetic apparatus. These changes can serve two purposes: to provide extra amino-acids and to decrease excitation pressure. We examined the effects of nitrogen limitation on the form and function of the photosynthetic apparatus. Our aim was to study which of the two demands serve as the driving force for the remodeling of the photosynthetic apparatus, under different growth conditions. We found that a drastic reduction in light intensity allowed cells to maintain a more functional photosynthetic apparatus: the phycobilisome antenna was bigger, the activity of both photosystems was higher and the levels of photosystem (PS) proteins were higher. Pre-acclimating cells to Mn limitation, under which the activity of both PSI and PSII is diminished, results in a very similar response. The rate of PSII photoinhibition, in nitrogen limited cells, was found to be directly related to the activity of the photosynthetic apparatus. These data indicate that, under our experimental conditions, photo-damage avoidance was the more prominent determinant during the acclimation process. The combinations of limiting factors tested here is by no means artificial. Similar scenarios can take place under environmental conditions and should be taken into account when estimating nutrient limitations in nature.

Analysis of heterologous regulatory and coding regions in algal chloroplasts

The basic photosynthetic apparatus is highly conserved across all photosynthetic organisms, and this conservation can be seen in both protein composition and amino acid sequence. Conservation of regulatory elements also seems possible in chloroplast genes, as many mRNA untranslated regions (UTRs) appear to have similar structural elements. The D1 protein of Photosystem II (psbA gene) is a highly conserved core reaction center protein that shows very similar regulation from cyanobacteria through higher plants. We engineered full and partial psbA genes from a diverse set of photosynthetic organisms into a psbA deficient strain of Chlamydomonas reinhardtii. Analysis of D1 protein accumulation and photosynthetic growth revealed that coding sequences and promoters are interchangeable even between anciently diverged species. On the other hand functional recognition of 5' UTRs is limited to closely related organisms. Furthermore transformation of heterologous promoters and 5' UTRs from the atpA, tufA and psbD genes conferred psbA mRNA accumulation but not translation. Overall, our results show that heterologous D1 proteins can be expressed and complement Photosystem II function in green algae, while RNA regulatory elements appear to be very specific and function only from closely related species. Nonetheless, there is great potential for the expression of heterologous photosynthetic coding sequences for studying and modifying photosynthesis in C. reinhardtii chloroplasts.

Thermal Acclimation of the Symbiotic Alga Symbiodinium spp. Alleviates Photobleaching under Heat Stress

A moderate increase in seawater temperature causes coral bleaching, at least partially through photobleaching of the symbiotic algae Symbiodinium spp. Photobleaching of Symbiodinium spp. is primarily associated with the loss of light-harvesting proteins of photosystem II (PSII) and follows the inactivation of PSII under heat stress. Here, we examined the effect of increased growth temperature on the change in sensitivity of Symbiodinium spp. PSII inactivation and photobleaching under heat stress. When Symbiodinium spp. cells were grown at 25°C and 30°C, the thermal tolerance of PSII, measured by the thermal stability of the maximum quantum yield of PSII in darkness, was commonly enhanced in all six Symbiodinium spp. tested. In Symbiodinium sp. CCMP827, it took 6 h to acquire the maximum PSII thermal tolerance after transfer from 25°C to 30°C. The effect of increased growth temperature on the thermal tolerance of PSII was completely abolished by chloramphenicol, indicating that the acclimation mechanism of PSII is associated with the de novo synthesis of proteins. When CCMP827 cells were exposed to light at temperature ranging from 25°C to 35°C, the sensitivity of cells to both high temperature-induced photoinhibition and photobleaching was ameliorated by increased growth temperatures. These results demonstrate that thermal acclimation of Symbiodinium spp. helps to improve the thermal tolerance of PSII, resulting in reduced inactivation of PSII and algal photobleaching. These results suggest that whole-organism coral bleaching associated with algal photobleaching can be at least partially suppressed by the thermal acclimation of Symbiodinium spp. at higher growth temperatures.

Synthetic Oligonucleotide Libraries Reveal Novel Regulatory Elements in Chlamydomonas Chloroplast mRNAs

Gene expression in chloroplasts is highly regulated during translation by sequence and secondary-structure elements in the 5' untranslated region (UTR) of mRNAs. These chloroplast mRNA 5' UTRs interact with nuclear-encoded factors to regulate mRNA processing, stability, and translation initiation. Although several UTR elements in chloroplast mRNAs have been identified by site-directed mutagenesis, the complete set of elements required for expression of plastid mRNAs remains undefined. Here we present a synthetic biology approach using an arrayed oligonucleotide library to examine in vivo hundreds of designed variants of endogenous UTRs from Chlamydomonas reinhardtii and quantitatively identify essential regions through next-generation sequencing of thousands of mutants. We validate this strategy by characterizing the relatively well-studied 5' UTR of the psbD mRNA encoding the D2 protein in photosystem II and find that our analysis generally agrees with previous work identifying regions of importance but significantly expands and clarifies the boundaries of these regulatory regions. We then use this strategy to characterize the previously unstudied psaA 5' UTR and obtain a detailed map of regions essential for both positive and negative regulation. This analysis can be performed in a high-throughput manner relative to previous site-directed mutagenesis methods, enabling compilation of a large unbiased data set of regulatory elements of chloroplast gene expression. Finally, we create a novel synthetic UTR based on aggregate sequence analysis from the libraries and demonstrate that it significantly increases accumulation of an exogenous protein, attesting to the utility of this strategy for enhancing protein production in algal chloroplasts.

Psb28 is involved in recovery of photosystem II at high temperature in Synechocystis sp. PCC 6803

Psb28 is an extrinsic protein of photosystem II (PSII), which is conserved among photosynthetic organisms from cyanobacteria to higher plants. A unicellular cyanobacterium, Synechocystis sp. PCC 6803, has two homologs of Psb28, Psb28-1 and Psb28-2. However, the role of these proteins remains poorly understood. In this study, we disrupted the psb28-1 (sll1398) and psb28-2 (slr1739) genes in wild-type Synechocystis sp. PCC 6803 and examined their photosynthetic properties to elucidate the physiological role of Psb28 in photosynthesis. We also disrupted the psb28-1 gene in a dgdA mutant defective in the biosynthesis of digalactosyldiacylglycerol, in which Psb28-1 significantly accumulates in PSII. The disruption of the psb28-1 gene in the wild-type resulted in growth retardation under high-light conditions at high temperatures with a low rate of restoration of photodamaged photosynthetic machinery. Similar phenomena were observed at normal growth temperatures in the psb28-1/dgdA double mutant. In contrast, disruption of psb28-2 in the wild-type and dgdA mutant did not affect host strain phenotype, suggesting that Psb28-2 does not contribute to the recovery of PSII. In addition, protein analysis using strains expressing His-tagged Psb28-1 revealed that Psb28-1 is mainly associated with the CP43-less PSII monomer. In the dgdA mutant, the CP43-less PSII monomer accumulated to a greater extent than in the wild-type, and its accumulation caused greater accumulation of Psb28-1 in PSII. These results demonstrate that Psb28-1 plays an important role in PSII repair through association with the CP43-less monomer, particularly at high temperatures.

UV-B radiation: “When does the stressor cause stress?”

Exposure to UV-B radiation can cause stress in plants Solar UV-B radiation (280 315 nm) has long been recognized as being potentially damaging to living organisms. Indeed, the literature on plant UV-B radiation effects has for decades been dominated by reports on UV-B mediated stress, including growth retardation, macroscopic injuries and oxidative damage (Caldwell et al., 1994; Searles et al., 2001). These negative effects comprise damaging effects on genetic material (formation pre-mutagenic cyclobutane pyrimidine dimers [CPD] and pyrimidine [6-4] pyrimidinone dimers), photosynthetic performance (in-tandem degradation of D1-D2 core proteins of photosystem II, inactivation RUBISCO, altered stomatal function) and a range of other cellular targets (see Jansen et al., 1998; Searles et al., 2001; Jordan 2002; Rozema et al., 2005; Jenkins, 2009). In this issue Lidon et al. (2012a) review our current understanding of the deleterious effects of UV-B on photosynthesis. UV-B damage is paralleled by the formation of lipid peroxidation products such as malondialdehyde (MDA) (Hideg et al., 2003; Lidon and Ramalho, 2011) and increased oxidation of antioxidants such as glutathione (Kalbin et al., 1997), both of which reflect the oxidative character of the UV-caused stress conditions. Consistently, UV-induced ROS have been measured using EPR spin trap reporters in both leaves (Hideg and Vass, 1996) and in isolated thylakoids (Lidon et al., 2012b) exposed to high doses of UV-B.