Dataset Information

Synechococcus IBT LC-MS/MS - Proteomic Response to Rising Temperature in the Marine Cyanobacterium Synechococcus Grown in Different Nitrogen Sources

ABSTRACT: we investigated molecular response of an oceanic Synechococcus strain WH 8102 grown on two nitrogen sources (nitrate and urea) under present (25°C) and predicted future (28°C) temperature conditions using an IBT-based quantitative proteomic approach.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Synechococcus Sp. (strain Wh8102)

SUBMITTER: Yuan-Yuan Li

LAB HEAD: Da-Zhi Wang

PROVIDER: PXD011884 | Pride | 2019-08-19

REPOSITORIES: Pride

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Proteomic Response to Rising Temperature in the Marine Cyanobacterium Synechococcus Grown in Different Nitrogen Sources.

Li Yuan-Yuan YY Chen Xiao-Huang XH Xue Cheng C Zhang Hao H Sun Geng G Xie Zhang-Xian ZX Lin Lin L Wang Da-Zhi DZ

Frontiers in microbiology 20190823

Synechococcus is one of the most important contributors to global primary productivity, and ocean warming is predicted to increase abundance and distribution of Synechococcus in the ocean. Here, we investigated molecular response of an oceanic Synechococcus strain WH8102 grown in two nitrogen sources (nitrate and urea) under present (25°C) and predicted future (28°C) temperature conditions using an isobaric tag (IBT)-based quantitative proteomic approach. Rising temperature ...[more]

PMID: 31507578

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Project description:Phosphorylation is a regulatory mechanism by which intracellular apicomplexan parasites control the process of invading and modifying host cells. However, the sporulated oocysts’ phosphoprotein repertoires between virulent and avirulent strains of Toxoplasma gondii and the underlying mechanisms contributing to virulence is still a mystery. A quantitative analysis of the sporulated oocysts’ phosphoproteome profile of T. gondii virulent and avirulent strains belonging to different genotypes was conducted to reveal phosphoprotein expression patterns that contribute to the virulence of a particular phenotype. Phosphopeptides from the sporulated oocysts of the virulent strain PYS (Chinese ToxoDB#9) and the avirulent strain type II (PRU strain) were enriched by titanium dioxide (TiO2) affinity chromatography and quantified using iBT technology. A total of 10,645 unique phosphopeptides, 8,181 nonredundant phosphorylation sites and 2,792 phosphoproteins were identified. The quantitative analysis identified 4,129 differentially expressed phosphopeptides (DEPs) between sporulated oocysts of the PYS strain and PRU strain (|log1.5 fold change| > 1 and P < 0.05), including 2,485 upregulated and 1,644 downregulated phosphopeptides. Motif analysis identified 24 motifs from the upregulated phosphorylated peptides including 22 serine motifs and two threonine motifs (TPE and TP), and 15 motifs from the downregulated phosphorylated peptides including 12 serine motifs and three threonine motifs (TP, RxxT and KxxT) in PYS strain when comparing PYS/PRU. Several kinases were consistent with motifs of overrepresented phosphopeptides, such as PKA, PKG, CKII, IKK, MAPK, EGFR, INSR, Jak, Syk, Src, Ab1. GO analysis, KEGG pathway analysis and STRING analysis revealed differentially expressed phosphoproteins (DEPs) exhibiting significant functional properties. Kinase associated network analysis showed that AGC kinase had the greatest connected peptides. Our findings reveal significant difference in phosphopeptides of sporulated oocysts between virulent and avirulent T. gondii strains, which provides solid foundation for further exploring the mechanisms contributing to the virulence of T. gondii.

Project description:Proteins secreted by marine cyanobacterium Synechococcus under phosphorus stress is largely uncharacterized. This dataset characterizes the exoproteins for both an open ocean (WH8102) and coastal (WH5701) Synechococcus strain and were collected as part of the study "Dissolved organic phosphorus bond-class utilization by Synechococcus". Study Abstract: Dissolved organic phosphorus (DOP) contains compounds with phosphoester (P-O-C), phosphoanhydride (P-O-P), and phosphorus-carbon (P-C) bonds. Despite DOP’s importance as a nutritional source for marine microorganisms, the bioavailability of each bond-class to the widespread cyanobacterium Synechococcus remains largely unknown. This study evaluates bond-class specific DOP utilization by cultures of an open ocean and a coastal ocean Synechococcus strain. Both strains exhibited comparable growth rates when provided phosphate, short-chain and long-chain polyphosphate (P-O-P), adenosine 5’-triphosphate (P-O-C and P-O-P), and glucose-6-phosphate (P-O-C) as the phosphorus source. However, growth rates on phosphomonoester adenosine 5’-monophosphate (P-O-C) and phosphodiester bis(4-methylumbelliferyl) phosphate (C-O-P-O-C) varied between strains, and neither strain grew on selected phosphonates. Consistent with the growth measurements, both strains preferentially hydrolyzed 3-polyphosphate, followed by adenosine 5’-triphosphate, and then adenosine 5’-monophosphate. The strains’ exoproteome contained phosphorus hydrolases, which combined with enhanced cell-free hydrolysis of 3-polyphosphate and adenosine 5’-triphosphate under phosphate deficiency, suggests active mineralization of short-chain polyphosphate by Synechococcus’ exoproteins. Synechococcus alkaline phosphatases presented broad substrate specificities, including activity towards short-chain polyphosphate, with varying affinities between the two strains. Collectively, these findings underscore the potentially significant role of compounds with phosphoanhydride bonds in Synechococcus phosphorus nutrition, thereby expanding our understanding of microbially-mediated DOP cycling in marine ecosystems.

Project description:Biological CO2 mitigation by photosynthetic microorganisms has emerged as a promising approach for generating biomass-based energy during the course of CO2 fixation. Additionally, cyanobacteria-based biofuels have also garnered immense attention lately because of the depleting fossil fuel reserves and the growing energy demands. Synechococcus elongatus PCC 11801, a fast-growing, high CO2 tolerant, novel isolate of cyanobacteria, is an interesting candidate for metabolic engineering applications. Since under laboratory conditions, it exhibited a high level of tolerance to different environmental stresses (CO2, light, temperature, salts and butanol), it seemed like an encouraging prospect for the production of fuels and other industrially relevant chemicals. This is the first-ever functional global proteomics investigation of Synechococcus elongatus PCC 11801 isolate grown at elevated CO2 levels using high-throughput iTRAQ approach. Three independent biological replicates were analyzed and a total of 861 proteins were identified, out of which 492 proteins were found to be present in all the three replicates. Of these, 248 proteins showing the same trend across the three replicates (≥1.5 fold up-regulation or ≤0.66 fold down-regulation) were chosen for pathway analysis. The metabolic responses were marked with a down-regulation of inorganic carbon transporters alongside an induction of nitrogen transport and absorption proteins in order to uphold the apposite carbon-nitrogen equilibrium. Further acclimation progression exposed an increased expression of proteins taking part in photosynthesis and generation of light harvesting pigments such as chlorophyll. Similarly, a downshift of proteins involved in photoprotection and defense against ROS (reactive oxygen species) was observed. Another principal discovery was the perturbation in expression of proteins belonging to central metabolic pathways like glycolysis, TCA cycle, pentose phosphate pathway as a coping mechanism to high CO2 stress. Further, validation studies were carried out using MRM assays and western blotting of key altered proteins.

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Dataset Information

Synechococcus IBT LC-MS/MS - Proteomic Response to Rising Temperature in the Marine Cyanobacterium Synechococcus Grown in Different Nitrogen Sources

Dataset's files

Publications

Proteomic Response to Rising Temperature in the Marine Cyanobacterium <i>Synechococcus</i> Grown in Different Nitrogen Sources.

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