ABSTRACT
Photosynthesis converting solar energy to chemical energy is one of the most important chemical reactions on earth. In cyanobacteria, light energy is captured by antenna system phycobilisomes (PBSs) and transferred to photosynthetic reaction centers of photosystem II (PSII) and photosystem I (PSI). While most of the protein complexes involved in photosynthesis have been characterized by in vitro structural analyses, how these protein complexes function together in vivo is not well understood. Here we implemented STAgSPA, an in situ structural analysis strategy, to solve the native structure of PBS-PSII supercomplex from the cyanobacteria Arthrospira sp. FACHB439 at resolution of ~3.5 Å. The structure reveals coupling details among adjacent PBSs and PSII dimers, and the collaborative energy transfer mechanism mediated by multiple super-PBS in cyanobacteria. Our results provide insights into the diversity of photosynthesis-related systems between prokaryotic cyanobacteria and eukaryotic red algae but are also a methodological demonstration for high-resolution structural analysis in cellular or tissue samples.
Subject(s)
Cyanobacteria , Photosystem II Protein Complex , Phycobilisomes , Phycobilisomes/metabolism , Phycobilisomes/chemistry , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/chemistry , Cyanobacteria/metabolism , Photosynthesis , Bacterial Proteins/metabolism , Bacterial Proteins/chemistry , Photosystem I Protein Complex/metabolism , Photosystem I Protein Complex/chemistry , Energy Transfer , Models, Molecular , Cryoelectron MicroscopyABSTRACT
Photosystem II (PSII) catalyzes the light-driven charge separation and water oxidation reactions of photosynthesis. Eukaryotic PSII core is usually associated with membrane-embedded light-harvesting antennae, which greatly increase the absorbance cross-section of the core. The peripheral antennae in different phototrophs vary considerably in protein composition and arrangement. Photosynthetic cryptophytes possess chlorophyll a/c binding proteins (CACs) that serve as their antennae. How these CACs assemble with the PSII core remains unclear. Here, we report the 2.57-Å resolution structure of cryptophyte PSII-CAC purified from cells at nitrogen-limited stationary growth phase. We show that each monomer of the PSII homodimer contains a core complex, six chlorophyll a/c binding proteins (CACs) and a previously unseen chlorophyll-binding protein (termed CAL-II). Six CACs are arranged as a double-layered arc-shaped non-parallel belt, and two such belts attach to the dimeric core from opposite sides. The CAL-II simultaneously interacts with a number of core subunits and five CACs. The distinct organization of CACs and the presence of CAL-II may play a critical role in stabilizing the dimeric PSII-CAC complex under stress conditions. Our study provides mechanistic insights into the assembly and function of the PSII-CAC complex as well as the possible adaptation of cryptophytes in response to environmental stresses.
Subject(s)
Cryptophyta , Photosystem II Protein Complex , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/chemistry , Cryptophyta/metabolism , Chlorophyll Binding Proteins/metabolism , Chlorophyll Binding Proteins/chemistry , Photosynthesis , Models, Molecular , Light-Harvesting Protein Complexes/metabolism , Light-Harvesting Protein Complexes/chemistryABSTRACT
Cyanobacteria are important targets for biotechnological applications due to their ability to grow in a wide variety of environments, rapid growth rates, and tractable genetic systems. They and their bioproducts can be used as bioplastics, biofertilizers, and in carbon capture and produce important secondary metabolites that can be used as pharmaceuticals. However, the photosynthetic process in cyanobacteria can be limited by a wide variety of environmental factors such as light intensity and wavelength, exposure to UV light, nutrient limitation, temperature, and salinity. Carefully considering these limitations, modifying the environment, and/or selecting cyanobacterial species will allow cyanobacteria to be used in biotechnological applications.
Subject(s)
Cyanobacteria , Photosystem I Protein Complex , Photosystem II Protein Complex , Cyanobacteria/metabolism , Cyanobacteria/genetics , Photosystem I Protein Complex/metabolism , Photosystem I Protein Complex/genetics , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/genetics , Photosynthesis , Light , Temperature , Ultraviolet Rays , Biotechnology/methodsABSTRACT
Singlet oxygen (1O2) is an important reactive oxygen species whose formation by the type-II, light-dependent, photodynamic reaction is inevitable during photosynthetic processes. In the last decades, the recognition that 1O2 is not only a damaging agent, but can also affect gene expression and participates in signal transduction pathways has received increasing attention. However, contrary to several other taxa, 1O2-responsive genes have not been identified in the important cyanobacterial model organism Synechocystis PCC 6803. By using global transcript analysis we have identified a large set of Synechocystis genes, whose transcript levels were either enhanced or repressed in the presence of 1O2. Characteristic 1O2 responses were observed in several light-inducible genes of Synechocystis, especially in the hli (or scp) family encoding HLIP/SCP proteins involved in photoprotection. Other important 1O2-induced genes include components of the Photosystem II repair machinery (psbA2 and ftsH2, ftsH3), iron homeostasis genes isiA and idiA, the group 2 sigma factor sigD, some components of the transcriptomes induced by salt-, hyperosmotic and cold-stress, as well as several genes of unknown function. The most pronounced 1O2-induced upregulation was observed for the hliB and the co-transcribed lilA genes, whose deletion induced enhanced sensitivity against 1O2-mediated light damage. A bioreporter Synechocystis strain was created by fusing the hliB promoter to the bacterial luciferase (lux), which showed its utility for continuous monitoring of 1O2 concentrations inside the cell.
Subject(s)
Bacterial Proteins , Gene Expression Regulation, Bacterial , Photosystem II Protein Complex , Singlet Oxygen , Synechocystis , Synechocystis/genetics , Synechocystis/metabolism , Singlet Oxygen/metabolism , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/genetics , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Light , Photosynthesis/geneticsABSTRACT
In recent years, inorganic nanoparticles, including calcium hydroxide nanoparticles [Ca Ca(OH)2 NPs], have attracted significant interest for their ability to impact plant photosynthesis and boost agricultural productivity. In this study, the effects of 15 and 30 mg L-1 oleylamine-coated calcium hydroxide nanoparticles [Ca(OH)2@OAm NPs] on photosystem II (PSII) photochemistry were investigated on tomato plants at their growth irradiance (GI) (580 µmol photons m-2 s-1) and at high irradiance (HI) (1000 µmol photons m-2 s-1). Ca(OH)2@OAm NPs synthesized via a microwave-assisted method revealed a crystallite size of 25 nm with 34% w/w of oleylamine coater, a hydrodynamic size of 145 nm, and a ζ-potential of 4 mV. Compared with the control plants (sprayed with distilled water), PSII efficiency in tomato plants sprayed with Ca(OH)2@OAm NPs declined as soon as 90 min after the spray, accompanied by a higher excess excitation energy at PSII. Nevertheless, after 72 h, the effective quantum yield of PSII electron transport (ΦPSII) in tomato plants sprayed with Ca(OH)2@OAm NPs enhanced due to both an increase in the fraction of open PSII reaction centers (qp) and to the enhancement in the excitation capture efficiency (Fv'/Fm') of these centers. However, the decrease at the same time in non-photochemical quenching (NPQ) resulted in an increased generation of reactive oxygen species (ROS). It can be concluded that Ca(OH)2@OAm NPs, by effectively regulating the non-photochemical quenching (NPQ) mechanism, enhanced the electron transport rate (ETR) and decreased the excess excitation energy in tomato leaves. The delay in the enhancement of PSII photochemistry by the calcium hydroxide NPs was less at the GI than at the HI. The enhancement of PSII function by calcium hydroxide NPs is suggested to be triggered by the NPQ mechanism that intensifies ROS generation, which is considered to be beneficial. Calcium hydroxide nanoparticles, in less than 72 h, activated a ROS regulatory network of light energy partitioning signaling that enhanced PSII function. Therefore, synthesized Ca(OH)2@OAm NPs could potentially be used as photosynthetic biostimulants to enhance crop yields, pending further testing on other plant species.
Subject(s)
Calcium Hydroxide , Nanoparticles , Photosystem II Protein Complex , Solanum lycopersicum , Photosystem II Protein Complex/metabolism , Calcium Hydroxide/chemistry , Nanoparticles/chemistry , Solanum lycopersicum/drug effects , Solanum lycopersicum/metabolism , Photosynthesis/drug effects , Hormesis , Electron Transport/drug effects , Reactive Oxygen Species/metabolismABSTRACT
BACKGROUND: The escalating impacts of global warming intensify the detrimental effects of heat stress on crop growth and yield. Among the earliest and most vulnerable sites of damage is Photosystem II (PSII). Plants exposed to recurring high temperatures develop heat stress memory, a phenomenon that enables them to retain information from previous stress events to better cope with subsequent one. Understanding the components and regulatory networks associated with heat stress memory is crucial for the development of heat-resistant crops. RESULTS: Physiological assays revealed that heat priming (HP) enabled tall fescue to possess higher Photosystem II photochemical activity when subjected to trigger stress. To investigate the underlying mechanisms of heat stress memory, we performed comparative proteomic analyses on tall fescue leaves at S0 (control), R4 (primed), and S5 (triggering), using an integrated approach of Tandem Mass Tag (TMT) labeling and Liquid Chromatography-Mass Spectrometry. A total of 3,851 proteins were detected, with quantitative information available for 3,835 proteins. Among these, we identified 1,423 differentially abundant proteins (DAPs), including 526 proteins that were classified as Heat Stress Memory Proteins (HSMPs). GO and KEGG enrichment analyses revealed that the HSMPs were primarily associated with the "autophagy" in R4 and with "PSII repair", "HSP binding", and "peptidase activity" in S5. Notably, we identified 7 chloroplast-localized HSMPs (HSP21, DJC77, EGY3, LHCA4, LQY1, PSBR and DEGP8, R4/S0 > 1.2, S5/S0 > 1.2), which were considered to be effectors linked to PSII heat stress memory, predominantly in cluster 4. Protein-protein interaction (PPI) analysis indicated that the ubiquitin-proteasome system, with key nodes at UPL3, RAD23b, and UCH3, might play a role in the selective retention of memory effectors in the R4 stage. Furthermore, we conducted RT-qPCR validation on 12 genes, and the results showed that in comparison to the S5 stage, the R4 stage exhibited reduced consistency between transcript and protein levels, providing additional evidence for post-transcriptional regulation in R4. CONCLUSIONS: These findings provide valuable insights into the establishment of heat stress memory under recurring high-temperature episodes and offer a conceptual framework for breeding thermotolerant crops with improved PSII functionality.
Subject(s)
Heat-Shock Response , Photosystem II Protein Complex , Proteomics , Thermotolerance , Photosystem II Protein Complex/metabolism , Proteomics/methods , Festuca/metabolism , Festuca/genetics , Plant Proteins/metabolism , Plant Proteins/genetics , Gene Expression Regulation, Plant , Proteome/metabolismABSTRACT
Photosynthesis is the main source of energy for plants to sustain growth and development. Abnormalities in photosynthesis may cause defects in plant development. The elaborate regulatory mechanism underlying photosynthesis remains unclear. In this study, we identified a natural mutant from the Greater Khingan Mountains and named it as "1-T". This mutant had variegated leaf with irregular distribution of yellow and green. Chlorophyll contents and photosynthetic capacity of 1-T were significantly reduced compared to other poplar genotypes. Furthermore, a transcriptome analysis revealed 3269 differentially expressed genes (DEGs) in 1-T. The products of the DEGs were enriched in photosystem I and photosystem II. Three motifs were significantly enriched in the promoters of these DEGs. Yeast one-hybrid, Electrophoretic mobility shift assays and tobacco transient transformation experiments indicated that PdGLKs may bind to the three motifs. Further analysis indicated that these photosystem related genes were also significantly down-regulated in PdGLK-RNAi poplars. Therefore, we preliminarily concluded that the down-regulation of PdGLKs in 1-T may affect the expression of photosystem-related genes, resulting in abnormal photosystem development and thus affecting the growth and development. Our results provide new insights into the molecular mechanism of photosynthesis regulating plant growth.
Subject(s)
Gene Expression Profiling , Photosynthesis , Populus , Populus/genetics , Populus/metabolism , Populus/growth & development , Photosynthesis/genetics , Gene Expression Regulation, Plant , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/genetics , Transcriptome , Photosystem I Protein Complex/metabolism , Photosystem I Protein Complex/genetics , Mutation , Plant Proteins/genetics , Plant Proteins/metabolismABSTRACT
The structure and mechanism of the water-oxidation chemistry that occurs in photosystem II have been subjects of great interest. The advent of X-ray free electron lasers allowed the determination of structures of the stable intermediate states and of steps in the transitions between these intermediate states, bringing a new perspective to this field. The room-temperature structures collected as the photosynthetic water oxidation reaction proceeds in real time have provided important novel insights into the structural changes and the mechanism of the water oxidation reaction. The time-resolved measurements have also given us a view of how this reaction-which involves multielectron, multiproton processes-is facilitated by the interaction of the ligands and the protein residues in the oxygen-evolving complex. These structures have also provided a picture of the dynamics occurring in the channels within photosystem II that are involved in the transport of the substrate water to the catalytic center and protons to the bulk.
Subject(s)
Lasers , Photosystem II Protein Complex , Photosystem II Protein Complex/chemistry , Photosystem II Protein Complex/ultrastructure , Photosystem II Protein Complex/metabolism , Electrons , Water/chemistry , Water/metabolism , X-Rays , Oxidation-Reduction , Models, MolecularABSTRACT
Amaranthus retroflexus L. (redroot pigweed) is one of the most problematic weeds in maize, sugar beet, vegetables, and soybean crop fields in Europe. Two pigweed amaranth biotypes (R1 and R2) from the Czech Republic resistant to photosystem II (PSII)-inhibiting herbicides were analyzed in this study. This study aimed to identify the genetic mechanisms that underlie the resistance observed in the biotypes. Additionally, we also intended to establish the use of chlorophyll fluorescence measurement as a rapid and reliable method for confirming herbicide resistance in this weed species. Both biotypes analyzed showed high resistance factors in a dose-response study and were thus confirmed to be resistant to PSII-inhibiting herbicides. A sequence analysis of the D1 protein revealed a well-known Ser-Gly substitution at amino acid position 264 in both biotypes. Molecular docking studies, along with the wild-type and mutant D1 protein's secondary structure analyses, revealed that the S264G mutation did not reduce herbicide affinity but instead indirectly affected the interaction between the target protein and the herbicides. The current study identified the S264G mutation as being responsible for conferring herbicide resistance in the pigweed amaranth biotypes. These findings can provide a strong basis for future studies that might use protein structure and mutation-based approaches to gain further insights into the detailed mechanisms of resistance in this weed species. In many individuals from both biotypes, resistance at a very early stage (BBCH10) of plants was demonstrated several hours after the application of the active ingredients by the chlorophyll fluorescence method. The effective PS II quantum yield parameter can be used as a rapid diagnostic tool for distinguishing between sensitive and resistant plants on an individual level. This method can be useful for identifying herbicide-resistant weed biotypes in the field, which can help farmers and weed management practitioners develop more effective weed control tactics.
Subject(s)
Amaranthus , Herbicide Resistance , Herbicides , Photosystem II Protein Complex , Amaranthus/genetics , Amaranthus/drug effects , Amaranthus/growth & development , Herbicide Resistance/genetics , Herbicides/pharmacology , Czech Republic , Photosystem II Protein Complex/genetics , Photosystem II Protein Complex/metabolism , Plant Proteins/genetics , Plant Proteins/metabolism , Plant Weeds/genetics , Plant Weeds/drug effects , Molecular Docking Simulation , MutationABSTRACT
As a critical step in advancing the simulation of photosynthetic complexes, we present the Martini 3 coarse-grained (CG) models of key cofactors associated with light harvesting (LHCII) proteins and the photosystem II (PSII) core complex. Our work focuses on the parametrization of beta-carotene, plastoquinone/quinol, violaxanthin, lutein, neoxanthin, chlorophyll A, chlorophyll B, and heme. We derived the CG parameters to match the all-atom reference simulations, while structural and thermodynamic properties of the cofactors were compared to experimental values when available. To further assess the reliability of the parameterization, we tested the behavior of these cofactors within their physiological environments, specifically in a lipid bilayer and bound to photosynthetic complexes. The results demonstrate that our CG models maintain the essential features required for realistic simulations. This work lays the groundwork for detailed simulations of the PSII-LHCII super-complex, providing a robust parameter set for future studies.
Subject(s)
Light-Harvesting Protein Complexes , Molecular Dynamics Simulation , Photosynthesis , Photosystem II Protein Complex , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/chemistry , Light-Harvesting Protein Complexes/chemistry , Light-Harvesting Protein Complexes/metabolism , Chlorophyll/metabolism , Chlorophyll/chemistry , Thermodynamics , beta Carotene/chemistry , beta Carotene/metabolism , Lipid Bilayers/chemistry , Lipid Bilayers/metabolism , Heme/chemistry , Heme/metabolism , Chlorophyll A/chemistry , Chlorophyll A/metabolismABSTRACT
Photosynthesis system II (PS II) is an important target for the development of bioherbicides. In this study, a series of natural naphthoquinone derivatives containing diaryl ether were designed and synthesized based on the binding model of lawsone and PS II D1. Bioassays exhibited that most compounds had more than 80% inhibition of Portulaca oleracea and Echinochloa crusgalli roots at a dose of 100 µg/mL and compounds B4, B5, and C3 exhibited superior herbicidal activities against dicotyledonous and monocotyledon weeds to commercial atrazine. In particular, compound B5 exhibited excellent herbicidal activity at a dosage of 150 g a.i./ha. In addition, compared with atrazine, compound B5 causes less damage to crops. Molecular docking studies revealed that compound B5 effectively interacted with Pisum sativum PS II D1 via diverse interaction models, such as π-π stacking and hydrogen bonds. Molecular dynamics simulation studies and chlorophyll fluorescence measurements revealed that compound B5 acted on PS II. This is the first report of natural naphthoquinone derivatives targeting PS II and compound B5 may be a candidate molecule for the development of new herbicides targeting PS II.
Subject(s)
Drug Design , Echinochloa , Herbicides , Molecular Docking Simulation , Naphthoquinones , Plant Weeds , Herbicides/chemistry , Herbicides/pharmacology , Herbicides/chemical synthesis , Naphthoquinones/chemistry , Naphthoquinones/pharmacology , Echinochloa/drug effects , Echinochloa/growth & development , Plant Weeds/drug effects , Plant Weeds/growth & development , Structure-Activity Relationship , Ethers/chemistry , Ethers/pharmacology , Photosystem II Protein Complex/chemistry , Photosystem II Protein Complex/antagonists & inhibitors , Photosystem II Protein Complex/metabolism , Molecular Structure , Plant Proteins/chemistry , Plant Roots/chemistry , Plant Roots/drug effectsABSTRACT
Chlorophyll is essential in photosynthesis, converting sunlight into chemical energy in plants, algae, and certain bacteria. Its structure, featuring a porphyrin ring enclosing a central magnesium ion, varies in forms like chlorophyll a, b, c, d, and f, allowing light absorption at a broader spectrum. With a 20-carbon phytyl tail (except for chlorophyll c), chlorophyll is anchored to proteins. Previous findings suggested the presence of chlorophyll with a modified farnesyl tail in thermophilic cyanobacteria Thermosynechoccocus vestitus. In our Arabidopsis thaliana PSII cryo-EM map, specific chlorophylls showed incomplete phytyl tails, suggesting potential farnesyl modifications. However, further high-resolution mass spectrometry (HRMS) analysis in A. thaliana and T. vestitus did not confirm the presence of any farnesyl tails. Instead, we propose the truncated tails in PSII models may result from binding pocket flexibility rather than actual modifications.
Subject(s)
Arabidopsis , Chlorophyll , Photosystem II Protein Complex , Chlorophyll/metabolism , Photosystem II Protein Complex/metabolism , Arabidopsis/metabolism , Mass Spectrometry , Thermosynechococcus/metabolism , Cryoelectron MicroscopyABSTRACT
This research aimed to develop natural plant systems to serve as biological sentinels for the detection of organophosphate pesticides in the environment. The working hypothesis was that the presence of the pesticide in the environment caused changes in the content of pigments and in the photosynthetic functioning of the plant, which could be evaluated non-destructively through the analysis of reflected light and emitted fluorescence. The objective of the research was to furnish in vivo indicators derived from spectroscopic parameters, serving as early alert signals for the presence of organophosphates in the environment. In this context, the effects of two pesticides, Chlorpyrifos and Dimethoate, on the spectroscopic properties of aquatic plants (Vallisneria nana and Spathyfillum wallisii) were studied. Chlorophyll-a variable fluorescence allowed monitoring both pesticides' presence before any damage was observed at the naked eye, with the analysis of the fast transient (OJIP curve) proving more responsive than Kautsky kinetics, steady-state fluorescence, or reflectance measurements. Pesticides produced a decrease in the maximum quantum yield of PSII photochemistry, in the proportion of PSII photochemical deexcitation relative to PSII non photochemical decay and in the probability that trapped excitons moved electrons into the photosynthetic transport chain beyond QA-. Additionally, an increase in the proportion of absorbed energy being dissipated as heat rather than being utilized in the photosynthetic process, was notorious. The pesticides induced a higher deactivation of chlorophyll excited states by photophysical pathways (including fluorescence) with a decrease in the quantum yields of photosystem II and heat dissipation by non-photochemical quenching. The investigated aquatic plants served as sentinels for the presence of pesticides in the environment, with the alert signal starting within the first milliseconds of electronic transport in the photosynthetic chain. Organophosphates damage animals' central nervous systems similarly to certain compounds found in chemical weapons, thus raising the possibility that sentinel plants could potentially signal the presence of such weapons.
Subject(s)
Chlorophyll , Chlorpyrifos , Chlorophyll/metabolism , Chlorophyll/chemistry , Chlorpyrifos/metabolism , Chlorpyrifos/toxicity , Fluorescence , Pesticides/toxicity , Pesticides/metabolism , Photosynthesis/drug effects , Dimethoate/toxicity , Dimethoate/metabolism , Spectrometry, Fluorescence , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/chemistry , Environmental Monitoring/methods , Chlorophyll A/metabolism , Chlorophyll A/chemistry , Kinetics , Water Pollutants, Chemical/analysis , Water Pollutants, Chemical/toxicity , Water Pollutants, Chemical/metabolismABSTRACT
The unprenylated benzoquinones 2,3,5,6-tetramethyl-1,4-benzoquinone (duroquinone), 2-chloro-1,4-benzoquinone (CBQ), 2,6-dimethyl-1,4-benzoquinone (DMBQ), 2,6-dichloro-1,4-benzoquinone (DCBQ), and 2,6-dimethoxy-1,4-benzoquinone (DMOBQ) were tested as putative antimetabolites of plastoquinone-9, a vital electron and proton carrier of oxygenic phototrophs. Duroquinone and CBQ were the most effective at inhibiting the growth of the cyanobacterium Synechocystis sp. PCC 6803 either in photomixotrophic or photoautotrophic conditions. Duroquinone, a close structural analog of the photosynthetic inhibitor methyl-plastoquinone-9, was found to possess genuine bactericidal activity towards Synechocystis at a concentration as low as 10 µM, while at the same concentration CBQ acted only as a mild bacteriostat. In contrast, only duroquinone displayed marked cytotoxicity in axenically-grown Arabidopsis, resulting in damages to photosystem II and hindered net CO2 assimilation. Metabolite profiling targeted to photosynthetic cofactors and pigments indicated that in Arabidopsis duroquinone does not directly inhibit plastoquinone-9 biosynthesis. Taken together, these data indicate that duroquinone offers prospects as an algicide and herbicide.
Subject(s)
Photosynthesis , Plastoquinone , Synechocystis , Plastoquinone/pharmacology , Plastoquinone/chemistry , Plastoquinone/metabolism , Photosynthesis/drug effects , Synechocystis/drug effects , Synechocystis/metabolism , Arabidopsis/drug effects , Arabidopsis/metabolism , Molecular Structure , Photosystem II Protein Complex/antagonists & inhibitors , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/drug effects , Anti-Bacterial Agents/pharmacology , Anti-Bacterial Agents/chemistryABSTRACT
Drought stress affects plant photosynthesis, leading to a reduction in the quality and yield of crop production. Non-foliar organs play a complementary role in photosynthesis during plant growth and development and are important sources of energy. However, there are limited studies on the performance of non-foliar organs under drought stress. The photosynthetic-responsive differences of oat spikelet organs (glumes, lemmas and paleas) and flag leaves to drought stress during the grain-filling stage were examined. Under drought stress, photosynthetic performance of glume is more stable. Intercellular CO2 concentration (Ci), chlorophyll b, maximum photochemical efficiency of photosystem II. (Fv/Fm), and electron transport rate (ETR) were significantly higher in the glume compared to the flag leaf. The transcriptome data revealed that stable expression of the RCCR gene under drought stress was the main reason for maintaining higher chlorophyll content in the glume. Additionally, no differential expression genes (DEGs) related to Photosystem â (PSI) reaction centers were found, and drought stress primarily affects the Photosystem II (PSII) reaction center. In spikelets, the CP43 and CP47 subunits of PSII and the AtpB subunit of ATP synthase were increased on the thylakoid membrane, contributing to photosynthetic stabilisation of spikelets as a means of supplementing the limited photosynthesis of the leaves under drought stress. The results enhanced understanding of the photosynthetic performance of oat spikelet during the grain-filling stage, and also provided an important basis on improving the photosynthetic capacity of non-foliar organs for the selection and breeding new oat varieties with high yield and better drought resistance.
Subject(s)
Avena , Droughts , Photosynthesis , Photosystem II Protein Complex , Photosynthesis/physiology , Avena/genetics , Avena/metabolism , Avena/growth & development , Avena/physiology , Photosystem II Protein Complex/metabolism , Chlorophyll/metabolism , Plant Leaves/metabolism , Plant Leaves/physiology , Stress, Physiological , Gene Expression Regulation, Plant , Photosystem I Protein Complex/metabolism , Edible Grain/physiology , Edible Grain/genetics , Edible Grain/growth & development , Edible Grain/metabolism , Plant Proteins/metabolism , Plant Proteins/geneticsABSTRACT
Global warming and increased atmospheric nitrogen (N) deposition can adversely impact Sphagnum moss populations and ecological functions in peatlands. Based on the anticipated increases in temperature and N levels at global scale, we investigated the effects of simultaneous warming and N treatment on growth and ecophysiological activity of Sphagnum papillosum, a predominant moss at mid-latitudes, utilizing a growth chamber experiment. Warming treatments increased the maximum yield of photosystem II (Fv/Fm) of S. papillosum while decreasing the stable carbon isotope ratio. However, warming treatment alone did not cause significant changes in the biomass increase from that of the control. Regarding N treatment, the low N treatment decreased Fv/Fm under the current temperature but did not affect the biomass increase. In contrast to these results, a simultaneous warming and high N treatment significantly enhanced the biomass production compared to that of the control, exhibiting additive effect of warming and high N treatment on Sphagnum biomass production. These responses were attributed to the improved photosynthetic performances by warming and N treatment. The results of this study contribute to the prediction of Sphagnum responses to warming and changes in N deposition.
Subject(s)
Biomass , Global Warming , Nitrogen , Photosynthesis , Sphagnopsida , Nitrogen/metabolism , Sphagnopsida/metabolism , Sphagnopsida/growth & development , Temperature , Carbon Isotopes , Photosystem II Protein Complex/metabolismABSTRACT
Drought stress caused by the global climate considerably disturbs plant yield and growth. Here, we explored the putative roles of silicon in repressing drought mechanisms in pepper and the prominent involvement of secondary metabolites, GA pathway, and photosystem II. Our research revealed that the transcript level of the flavonoid biosynthesis-associated genes, including the PAL, 4-CL, CHS, FLS-1, F3H and DFR, progressively induced in the pepper leaves treated with silicon during the drought stress duration. Moreover, the phenolic and flavonoid compounds extensively induced in the pepper plants. Furthermore, the pepper plants markedly inhibited chlorophyll catabolic-allied genes, senescence-related marker gene, and the Rbohs gene. Silicon application also sustained the membrane stability, supported via fewer electrolyte leakage processes and minor, O2- H2O2 and MDA levels during drought. Apart from this, the pepper plants significantly induced the expression level of the photosystem II-related genes, osmoprotectants pathway-associated genes, and antioxidant defense genes. Moreover, the GA biosynthesis genes were prompted, while the ABA signaling and biosynthesis genes were suppressed in the silicon-supplemented plants. These consequences infer that the role of Si supplementation on enhancing drought tolerance could be elucidated through the activation of secondary metabolites, flavonoid biosynthesis, osmoprotectants, GA pathway, the efficiency of PSII, and the suppression of chlorophyll degradation. Our research outcomes unveil new and remarkable characteristics of silicon supplementation and offer a series of candidate targets for improving the tolerance of pepper plants to drought stress.
Subject(s)
Capsicum , Chlorophyll , Drought Resistance , Silicon , Capsicum/metabolism , Capsicum/genetics , Capsicum/drug effects , Capsicum/physiology , Chlorophyll/metabolism , Chlorophyll/biosynthesis , Drought Resistance/drug effects , Gene Expression Regulation, Plant/drug effects , Photosystem II Protein Complex/metabolism , Plant Leaves/metabolism , Plant Leaves/drug effects , Silicon/pharmacology , Silicon/metabolismABSTRACT
Recent resolution advancement of in situ cryo-electron tomography (cryo-ET) and cryo-electron microscopy (cryo-EM) enables us to visualize large enzymes-in-action in atomic detail in their native environments inside living cells, such as photosystem II (PSII) and the ribosome. A variety of crystallographic and cryo-EM structures of PSII have been published for the purified PSII dimeric core complexes by itself, in supercomplexes with photosystem I (PSI) and light-harvesting complexes (LHC), and in megacomplexes with phycobilisome (PBS). In the latter case, two or five copies of asymmetric dimeric PSII molecules are present in highly asymmetric environments that differ from other 2-fold symmetric structures. Previous systematic analysis of X-ray free-electron laser (XFEL) crystal structures of PSII has shown different degrees of composition heterogeneity of metal ion cofactor bound at the oxygen-evolving center (OEC), including between two monomers of the same PSII dimer. This study analyzed the metal ions bound at four OECs in two asymmetric dimeric PSII molecules within in situ cryo-ET structures reported for an asymmetric PBS-PSII-PSI-LHC megacomplex determined in a living organism without purification and shows that composition heterogeneity with reduced metal ion occupancies at the OEC of PSII is a general phenomenon. This finding could have profound implications for spectroscopic interpretations of unpurified PSII samples.
Subject(s)
Oxygen , Photosystem II Protein Complex , Photosystem II Protein Complex/chemistry , Photosystem II Protein Complex/metabolism , Oxygen/metabolism , Oxygen/chemistry , Cryoelectron Microscopy , Models, Molecular , Thermosynechococcus/metabolism , Metals/metabolism , Metals/chemistry , Bacterial Proteins/chemistry , Bacterial Proteins/metabolismABSTRACT
BACKGROUND: Climate change exacerbates abiotic stresses, which are expected to intensify their impact on crop plants. Drought, the most prevalent abiotic stress, significantly affects agricultural production worldwide. Improving eggplant varieties to withstand abiotic stress is vital due to rising drought from climate change. Despite the diversity of wild eggplant species that thrive under harsh conditions, the understanding of their drought tolerance mechanisms remains limited. In the present study, we used chlorophyll fluorescence (ChlaF) imaging, which reveals a plant's photosynthetic health, to investigate desiccation tolerance in eggplant and its wild relatives. Conventional fluorescence measurements lack spatial heterogeneity, whereas ChlaF imaging offers comprehensive insights into plant responses to environmental stresses. Hence, employing noninvasive imaging techniques is essential for understanding this heterogeneity. RESULTS: Desiccation significantly reduced the leaf tissue moisture content (TMC) across species. ChlaF and TMC displayed greater photosystem II (PSII) efficiency after 54 h of desiccation in S. macrocarpum, S. torvum, and S. indicum, with S. macrocarpum demonstrating superior efficiency due to sustained fluorescence. PSII functions declined gradually in S. macrocarpum and S. torvum, unlike those in other species, which exhibited abrupt declines after 54 h of desiccation. However, after 54 h, PSII efficiency remained above 50% of its initial quantum yield in S. macrocarpum at 35% leaf RWC (relative water content), while S. torvum and S. indicum displayed 50% decreases at 31% and 33% RWC, respectively. Conversely, the susceptible species S. gilo and S. sisymbriifolium exhibited a 50% reduction in PSII function at an early stage of 50% RWC, whereas in S. melongena, this reduction occurred at 40% RWC. CONCLUSION: Overall, our study revealed notably greater leaf desiccation tolerance, especially in S. macrocarpum, S. torvum, and S. indicum, attributed to sustained PSII efficiency at low TMC levels, indicating that these species are promising sources of drought tolerance.
Subject(s)
Chlorophyll , Solanum melongena , Chlorophyll/metabolism , Fluorescence , Solanum melongena/physiology , Solanum melongena/metabolism , Plant Leaves/physiology , Plant Leaves/metabolism , Desiccation , Photosystem II Protein Complex/metabolism , Photosynthesis/physiology , Stress, Physiological , Droughts , Dehydration , Species SpecificityABSTRACT
Saline-sodic stress restricts the absorption of zinc by rice, consequently impacting the photosynthesis process of rice plants. In this experiment, Landrace 9 was selected as the test material and the potting method was employed to investigate the influence of ZnO nanoparticles (ZnO NPs) on zinc absorption and chlorophyll fluorescence in rice grown in saline-sodic land. The research findings demonstrate that the application of ZnO NPs proves to be more advantageous for the growth of rice in saline-sodic soil. Notably, the application of ZnO NPs significantly decreases the levels of Na+ and MDA in rice leaves in saline-sodic soil, while increasing the levels of K+ and Zn2+. Additionally, ZnO NPs enhances the content of chloroplast pigments, specific energy flux, quantum yield, and the performance of active PSII reaction center (PIABS) in rice leaves under saline-sodic stress. Furthermore, the relative variable fluorescence (WK and VJ) and quantum energy dissipation rate (φDo) of rice are also reduced. Therefore, the addition of ZnO NPs enhances the transfer of electrons and energy within the rice photosystem when subjected to saline-sodic stress. This promotes photosynthesis in rice plants growing in saline-sodic land, increasing their resistance to saline-sodic stress and ultimately facilitating their growth and development.