Dataset Information

Early Light-Inducible Protein (ELIP) Can Enhance Resistance to Cold-Induced Photooxidative Stress in Chlamydomonas reinhardtii.

ABSTRACT: Cold weather is one of the biggest challenges in establishing a large-scale microalgae culture facility in temperate regions. In order to develop a strain that is resistant to low temperatures and still maintains high photosynthetic efficiency, transgenic studies have been conducted targeting many genes. Early light-inducible proteins (ELIPs) located in thylakoid membranes are known to protect photosynthetic machinery from various environmental stresses in higher plants. An ELIP homolog was identified from Chlamydomonas reinhardtii and named ELIP3. The role of the gene was analyzed in terms of photosynthetic CO2 assimilation under cold stress. Western blot results showed a significant accumulation of ELIP3 when the cells were exposed to cold stress (4°C). High light stress alone did not induce the accumulation of the protein. Enhanced expression of ELIP3 helped survival of the cell under photo-oxidative stress. The influx of CO2 to the photobioreactor induced strong accumulation of ELIP3, and enhanced survival of the cell under high light and cold stress. When the oxidative stress was reduced by adding a ROS quencher, TEMPOL, to the media the expression of ELIP3 was reduced. A knockdown mutant showed much lower photosynthetic efficiency than wild type in low temperature, and died rapidly when it was exposed to high light and cold stress. The overexpression mutant survived significantly longer in the same conditions. Interestingly, knockdown mutants showed negative phototaxis, while the overexpression mutant showed positive phototaxis. These results suggest that ELIP3 may be involved in the regulation of the redox state of the cell and takes important role in protecting the photosystem under photooxidative stress in low temperatures.

SUBMITTER: Lee JW

PROVIDER: S-EPMC7478268 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Early Light-Inducible Protein (ELIP) Can Enhance Resistance to Cold-Induced Photooxidative Stress in <i>Chlamydomonas reinhardtii</i>.

Lee Ji Woong JW Lee Seung Hi SH Han Jong Won JW Kim Gwang Hoon GH

Frontiers in physiology 20200825

Cold weather is one of the biggest challenges in establishing a large-scale microalgae culture facility in temperate regions. In order to develop a strain that is resistant to low temperatures and still maintains high photosynthetic efficiency, transgenic studies have been conducted targeting many genes. Early light-inducible proteins (ELIPs) located in thylakoid membranes are known to protect photosynthetic machinery from various environmental stresses in higher plants. An <i>ELIP</i> homolog w ...[more]

PMID: 32982798

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Project description:Chlamydomonas reinhardtii is one of the most important model organisms nowadays phylogenetically situated between higher plants and animals (Merchant et al. 2007). Stress adaptation of this unicellular model algae is in the focus because of its relevance to biomass and biofuel production. Here, we have studied cold stress adaptation of C. reinhardtii hitherto not described for this algae whereas intensively studied in higher plants. Toward this goal, high throughput mass spectrometry was employed to integrate proteome, metabolome, physiological and cell-morphological changes during a time-course from 0 to 120 h. These data were complemented with RT-qPCR for target genes involved in central metabolism, signaling, and lipid biosynthesis. Using this approach dynamics in central metabolism were linked to cold-stress dependent sugar and autophagy pathways as well as novel genes in C. reinhardtii such as CKIN1, CKIN2 and a hitherto functionally not annotated protein named CKIN3. Cold stress affected extensively the physiology and the organization of the cell. Gluconeogenesis and starch biosynthesis pathways are activated leading to a pronounced starch and sugar accumulation. Quantitative lipid profiles indicate a sharp decrease in the lipophilic fraction and an increase in polyunsaturated fatty acids suggesting this as a mechanism of maintaining membrane fluidity. The proteome is completely remodeled during cold stress: specific candidates of the ribosome and the spliceosome indicate altered biosynthesis and degradation of proteins important for adaptation to low temperatures. Specific proteasome degradation may be mediated by the observed cold-specific changes in the ubiquitinylation system. Sparse partial least squares regression analysis was applied for protein correlation network analysis using proteins as predictors and Fv/Fm, FW, total lipids, and starch as responses. We applied also Granger causality analysis and revealed correlations between proteins and metabolites otherwise not detectable. Twenty percent of the proteins responsive to cold are uncharacterized proteins. This presents a considerable resource for new discoveries in cold stress biology in alga and plants.

Project description:BackgroundThe cellular proteome and metabolome are underlying dynamic regulation allowing rapid adaptation to changes in the environment. System-wide analysis of these dynamics will provide novel insights into mechanisms of stress adaptation for higher photosynthetic organisms. We applied pulsed-SILAC labeling to a photosynthetic organism for the first time and we established a method to study proteome dynamics in the green alga Chlamydomonas reinhardtii, an emerging model system for plant biology. In addition, we combined the analysis of protein synthesis with metabolic profiling to study the dynamic changes of metabolism and proteome turnover under salt stress conditions.ResultsTo study de novo protein synthesis an arginine auxotroph Chlamydomonas strain was cultivated in presence of stable isotope-labeled arginine for 24 hours. From the time course experiment in 3 salt concentrations we could identify more than 2500 proteins and their H/L ratio in at least one experimental condition; for 998 protiens at least 3 ratio counts were detected in the 24 h time point (0 mM NaCl). After fractionation we could identify 3115 proteins and for 1765 of them we determined their de novo synthesis rate. Consistently with previous findings we showed that RuBisCO is among the most prominent proteins in the cell; and similar abundance and turnover for the small and large RuBisCO subunit could be calculated. The D1 protein was identified among proteins with a high synthesis rates. A global median half-life of 45 h was calculated for Chlamydomonas proteins under the chosen conditions.ConclusionTo investigate the temporal co-regulation of the proteome and metabolome, we applied salt stress to Chlamydomonas and studied the time dependent regulation of protein expression and changes in the metabolome. The main metabolic response to salt stress was observed within the amino acid metabolism. In particular, proline was up-regulated manifold and according to that an increased carbon flow within the proline biosynthetic pathway could be measured. In parallel the analysis of abundance and de novo synthesis of the corresponding enzymes revealed that metabolic rearrangements precede adjustments of protein abundance.

Project description:BACKGROUND:Proteasomes remove regulatory proteins in eukaryotic cells, and control a variety of plant processes. Proteasomes are localized to the cytosol and nuclear, but their role in plant biology has recently been extended to chloroplasts, where it regulates TOC complex. This is turn controls the import of nuclear-encoded chloroplastic proteins, which remodels the chloroplast proteome and facilitates proper developmental transitions. Proteasomal regulation of the TOC complex also alleviates stressors that generate reactive oxygen species. These recent advances motivated us to determine if proteasome inhibition rapidly alters photosynthetic processes stemming from photoinhibition induced by high light. RESULTS:The short-term effects of proteasome inhibition on photosystem II during light stress was measured in Chlamydomonas reinhardtii, which allowed the dual monitoring of both chlorophyll fluorescence and cell viability. After 48?h at low light, proteasome inhibition did not affect viability or photochemistiry, but decreased cell concentration and increased cell volume. Two hours of high light stress impaired the efficiency of photosystem II in proteasome-inhibited cells, as determined by a decrease in Fv/Fm and the electron transport rate. Elevated photoinhibition in proteasome inhibited cells was not caused by a decrease in cell viability or chlorophyll content. Recovery from photoinhibition was attenuated in MG132-treated cells, and suppressed growth of a reestablished culture. Proteasome inhibition decreased de novo protein synthesis, which possibly constrained the ability to remodel the plastid proteome, and thus hampering the ability to adjust to high light stress. CONCLUSION:The proteasome is implicated in protecting photosystem II from photoinhibition. In addition to high light stress, other stressors- including metals, drought, and salt- are also known to generate reactive oxygen species localized to the chloroplast. Therefore, proteasome maintenance in plants may help protect photosynthesis during abiotic stress, which could increase crop yield during adverse conditions.

Dataset Information

Early Light-Inducible Protein (ELIP) Can Enhance Resistance to Cold-Induced Photooxidative Stress in Chlamydomonas reinhardtii.

Publications

Early Light-Inducible Protein (ELIP) Can Enhance Resistance to Cold-Induced Photooxidative Stress in <i>Chlamydomonas reinhardtii</i>.

Similar Datasets

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