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Synechocystis 6803 LC-MS/MS - Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins

ABSTRACT: Identification of the membrane and the soluble proteins in Synechocystis sp. PCC6803

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Synechocystis Sp. Pcc 6803

SUBMITTER: Yingchun Wang

LAB HEAD: Yingchun Wang

PROVIDER: PXD001246 | Pride | 2015-01-16

REPOSITORIES: Pride

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	GLY_M10_20140408.raw	Raw
	GLY_M11_20140408.raw	Raw
	GLY_M12_20140408.raw	Raw
	GLY_M1_20140408.raw	Raw
	GLY_M2_20140408.raw	Raw

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Publications

Systematically ranking the tightness of membrane association for peripheral membrane proteins (PMPs).

Gao Liyan L Ge Haitao H Huang Xiahe X Liu Kehui K Zhang Yuanya Y Xu Wu W Wang Yingchun Y

Molecular & cellular proteomics : MCP 20141213 2

Large-scale quantitative evaluation of the tightness of membrane association for nontransmembrane proteins is important for identifying true peripheral membrane proteins with functional significance. Herein, we simultaneously ranked more than 1000 proteins of the photosynthetic model organism Synechocystis sp. PCC 6803 for their relative tightness of membrane association using a proteomic approach. Using multiple precisely ranked and experimentally verified peripheral subunits of photosynthetic ...[more]

PMID: 25505158

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Project description:In this study, by using shotgun LC-MS/MS approach with the Tandem Mass Tag (TMTs) isobaric labelling technique we show that proteins in photosystem, inorganic carbon uptake and CO2 fixation systems are significantly changed in Δhik33 cells compared with WT cells.This is the normal culture condition proteomic data.

2017-05-19 | PXD005085 | Pride

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Proteomic comparison of HliD and Ycf39 protein abundances in FLAG-tagged chlorophyll synthase co-immunoprecipitation assays of control and CrtR/CruF (carotenoid biosynthesis) knockout strains of Synechocystis sp. PCC 6803.

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Phosphoproteome of the cyanobacterium Synechocystis sp. PCC 6803 and its dynamics during nitrogen starvation

Project description:Cyanobacteria have shaped the earth’s biosphere as the first oxygenic photoautotrophs and still play an important role in many ecosystems. The ability to adapt to changing environmental conditions is an essential characteristic in order to ensure survival. To this end, numerous studies have shown that bacteria use protein post-translational modifications such as Ser/Thr/Tyr phosphorylation in cell signalling, adaptation and regulation. Nevertheless, our knowledge of cyanobacterial phosphoproteomes and their dynamic response to environmental stimuli is relatively limited. In this study, we applied gel-free methods and high accuracy mass spectrometry towards the unbiased detection of Ser/Thr/Tyr phosphorylation events in the model cyanobacterium Synechocystis sp. PCC 6803. We could identify over 300 phosphorylation events in cultures grown on nitrate as exclusive nitrogen source. Chemical dimethylation labelling was applied to investigate proteome and phosphoproteome dynamics during nitrogen starvation. Our dataset describes the most comprehensive (phospho)proteome of Synechocystis to date, identifying 2,382 proteins and 183 phosphorylation events and quantifying 2,111 proteins and 148 phosphorylation events during nitrogen starvation. Global protein phosphorylation levels were increased in response to nitrogen depletion after 24 hours. Among the proteins with increased phosphorylation, the PII signalling protein showed the highest fold-change, serving as positive control. Other proteins with increased phosphorylation levels comprised functions in photosynthesis and in carbon and nitrogen metabolism. This study reveals dynamics of Synechocystis phosphoproteome in response to environmental stimuli and suggests an important role of protein Ser/Thr/Tyr phosphorylation in fundamental mechanisms of homeostatic control in cyanobacteria.

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Proximity labeling facilitates defining neighborhood proteome of photosystem II oxygen evolution complex in a model cyanobacterium

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