Dataset Information

Synechococcus elongatus PCC7942 proteome's cyclic rhythm by LC-MSMS

ABSTRACT: To uncover the variation in protein abundances during 48 hours under light and dark cycles (12:12-hours), we used quantitative proteomics, with TMT 6-plex isobaric labeling. We queried the S. elongatus proteome at ten different time points spanning a single 24 hour period, leading to 20 time points over the full 48 hour period.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Synechococcus Elongatus (strain Pcc 7942) (anacystis Nidulans R2)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Ana C. Guerreiro

LAB HEAD: Albert J.R. Heck

PROVIDER: PXD000510 | Pride | 2014-04-02

REPOSITORIES: Pride

ACCESS DATA

Publications

Daily rhythms in the cyanobacterium synechococcus elongatus probed by high-resolution mass spectrometry-based proteomics reveals a small defined set of cyclic proteins.

Guerreiro Ana C L AC Benevento Marco M Lehmann Robert R van Breukelen Bas B Post Harm H Giansanti Piero P Maarten Altelaar A F AF Axmann Ilka M IM Heck Albert J R AJ

Molecular & cellular proteomics : MCP 20140327 8

Circadian rhythms are self-sustained and adjustable cycles, typically entrained with light/dark and/or temperature cycles. These rhythms are present in animals, plants, fungi, and several bacteria. The central mechanism behind these "pacemakers" and the connection to the circadian regulated pathways are still poorly understood. The circadian rhythm of the cyanobacterium Synechococcus elongatus PCC 7942 (S. elongatus) is highly robust and controlled by only three proteins, KaiA, KaiB, and KaiC. T ...[more]

PMID: 24677030

Similar Datasets

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.

Dataset Information

Synechococcus elongatus PCC7942 proteome's cyclic rhythm by LC-MSMS

Publications

Daily rhythms in the cyanobacterium synechococcus elongatus probed by high-resolution mass spectrometry-based proteomics reveals a small defined set of cyclic proteins.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure