Ontology highlight
ABSTRACT:
PROVIDER: PRJNA962542 | ENA |
REPOSITORIES: ENA
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Project description:uncultured bacterium cbbL-ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit Raw sequence reads
| PRJNA765939 | ENA
Project description:uncultured bacterium cbbL-ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit Raw sequence reads
| PRJNA766221 | ENA
Project description:The impact of engineered nanomaterials intentionally or incidentally released in the environment on photosynthetic proteins remains largely unknown. Herein, we report positively charged iron oxide (Fe3O4) nanoparticles experience transformations in Arabidopsis thaliana plants in vivo that alter the formation and function of Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) protein corona, a key enzyme in the global carbon cycle. Elucidating rules of how nanoparticle properties and their transformations affect photosynthetic coronas will lead to more sustainable nanotechnology approaches for agriculture and the environment.
2025-03-04 | PXD055951 | JPOST Repository
Project description:Carbon dioxide is vital to the chemistry of life processes including including metabolism, cellular homeostasis, and pathogenesis. CO2 forms carbamates on the neutral N-terminal a-amino- and lysine e-amino-groups that regulate the activities of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin, however, very few protein other carbamates are known. Tools for the systematic identification of protein carbamylation sites have not been developed owing to the reversibility of carbamate formation, and in consequence carbamylation is typically overlooked. Here we demonstrate methods to identify protein carbamates using triethyloxonium ions to covalently trap CO2 on proteins for proteomic analysis. Our method delivers evidence to support the hypothesis that carbamylation is widespread in biology, and understanding its role should significantly advance our understanding of cellular CO2 interactions.
2018-10-23 | PXD007753 | Pride
Project description:Cyanidioschyzon merolae (C. merolae) is an acidophilic red alga growing in a naturally low carbon dioxide (CO2) environment. Although it uses a ribulose 1,5-bisphosphate carboxylase/oxygenase with high affinity for CO2, the survival of C. merolae relies on functional photorespiratory metabolism. In this study, we quantified the transcriptomic response of C. merolae to changes in CO2 conditions. We found distinct changes upon shifts between CO2 conditions, such as a concerted up-regulation of photorespiratory genes and responses to carbon starvation. We used the transcriptome data set to explore a hypothetical CO2 concentrating mechanism in C. merolae, based on the assumption that photorespiratory genes and possible candidate genes involved in a CO2 concentrating mechanism are co-expressed. A putative bicarbonate transport protein and two α-carbonic anhydrases were identified, which showed enhanced transcript levels under reduced CO2 conditions. Genes encoding enzymes of a PEP-CK-type C4 pathway were co-regulated with the photorespiratory gene cluster. We propose a model of a hypothetical low CO2 compensation mechanism in C. merolae integrating these low CO2-inducible components.
2017-07-31 | GSE100372 | GEO
Project description:The introduction of alternative CO2-fixing pathways such as formate synthesis and assimilation may improve the efficiency of biological carbon fixation that appears to be limited by the enzymatic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO). Here we aimed to establish a formate assimilation pathway in the model cyanobacterium Synechocystis sp. PCC 6803. The formate-tetrahydrofolate ligase (FTL) from Methylobacterium extorquens AM1 was expressed in Synechocystis to enable formate assimilation and reduce the loss of fixed carbon in the photorespiratory pathway. Transgenic strains accumulated serine and 3-phosphoglycerate, and consumed more 2-phosphoglycolate and glycine, which seemed to reflect the efficient utilization of formate. However, labelling experiments showed that the serine accumulation was not due to the expected incorporation of formate. DNA-microarray experiments were performed to analyze possible transcriptome changes due to ftl expression. Marked changes in expression of genes encoding proteins associated with serine biosynthesis and enzymes involved in nitrogen and C1 metabolism revealed that ftl expression had a regulatory impact on these metabolic routes. Our results indicate that the expression of new pathways could have a severe impact on the cellular regulatory network, which hampers the establishment of newly designed pathways.
2020-01-17 | GSE143785 | GEO
Project description:Random mutagenesis was applied to produce a new wheat mutant (RYNO3926) with superior characteristics regarding tolerance to water deficit treatment and rapid recovery from water stress conditions. Under water stress conditions mutant plants reached maturity faster and produced more seeds than its wild type wheat progenitor Further, whereas wild-type Tugela DN plants died within 7 days after induction of water stress, mutant plants survived by maintaining a higher relative moisture content (RMC), increased total chlorophyll, a higher photosynthesis rate and stomatal conductance suggesting that the mutant may possess a “stay green”’ phenotype. Analysis of the proteome of mutant plants revealed that they better regulate post-translational modification (SUMOylation) and have increased expression of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) proteins. Mutant plants also expressed unique proteins associated with dehydration tolerance including abscisic stress-ripening protein, cold induced protein, cold-responsive protein, dehydrin, Group 3 late embryogenesis and also a lipoprotein (LAlv9) belonging to the family of lipocalins. Overall, our results suggest that our new mutant RYNO3936 has a potential for inclusion in future breeding programs to improve drought tolerance under dryland conditions.
2021-09-09 | PXD019464 | Pride
Project description:Understanding the molecular differences in plant genotypes contrasting for heat sensitivity can provide useful insights into the mechanisms that confer heat tolerance in plants. This study is focused on comparative physiological and proteomic analyses of heat sensitive (ICC16374) and tolerant (JG14) genotypes of chickpea (Cicer arietinum L.) when subjected to heat stress at anthesis.Comparative gel-free proteome profiles indicated differences in the expression levels and regulation of common proteins that are associated with heat tolerance in contrasting genotypes under heat stress. The differentially regulated proteins were grouped into three categories based on their involvement in the molecular functions, cellular location and biological processes. Besides the identification of heat shock proteins, other proteins such as acetyl-CoA carboxylase, pyrroline-5-carboxylate synthase (P5CS), ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCo), phenylalanine ammonia-lyase (PAL) 2, ATP synthase, glycosyltransferase, sucrose synthase and late embryogenesis abundant (LEA) proteins were strongly associated with heat tolerance in chickpea. Several crucial proteins such as cystathionine gamma-synthase, glucose-1-phosphate adenyltransferas, malate dehydrogenase, threonine synthase, and non-cyanogenic ß-glucosidase were induced by heat only in the heat tolerant genotype. Based on pathway analysis, we propose that proteins which are essentially related to the electron transport chain in photosynthesis, aminoacid biosynthesis, ribosome synthesis and secondary metabolite synthesis may play key roles in inducing tolerance to heat stress.
2018-01-08 | PXD005578 | Pride
Project description:Cyanobacteria fix atmospheric CO2 to biomass and through metabolic engineering can also act as photosynthetic cell factories for sustainable productions of fuels and chemicals. The Calvin cycle is the primary pathway for CO2 fixation in cyanobacteria, algae and C3 plants, and several studies have shown that overexpression of a cyanobacterial Calvin cycle enzyme, bifunctional sedoheptulose-1,7-bisphosphatase/fructose-1,6-bisphosphatase (hereafter BiBPase), enhances CO2 fixation in both plants and algae, although its impact on cyanobacteria has not yet been rigorously studied. Here, we show that overexpression of BiBPase enhanced growth, cell size, and photosynthetic O2 evolution of the cyanobacterium Synechococcus sp. PCC 7002 in an environment with elevated CO2 concentration. Biochemical analysis, immunodetection, and proteomic analysis revealed that overexpression of BiBPase considerably elevated the cellular activities of two rate-limiting enzymes in the Calvin cycle, namely ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and aldolase, while it repressed several enzymes involved in the respiratory carbon metabolism (e.g. glycolysis and the oxidative pentose phosphate pathway) including glucose-6-phosphate dehydrogenase. Concomitantly, the content of glycogen was significantly reduced while the extracellular carbohydrate content increased. These results indicate that overexpression of BiBPase leads to global reprogramming of carbon metabolism in Synechococcus sp. PCC 7002, promoting photosynthetic carbon fixation and repressing the respiratory carbon catabolism, while altering carbohydrate partitioning.
2019-01-17 | PXD007963 | Pride