Dataset Information

Chemical profiling of live cell temporal redox dynamics in a photoautotrophic cyanobacterium

ABSTRACT: We have developed a quantitative chemical probe approach for live cell labeling of proteins that are sensitive to redox modifications. We utilize this in vivo strategy coupled to mass spectrometry-based proteomics to identify 176 proteins undergoing ~5-10 fold dynamic redox change in response to nutrient limitation and subsequent replenishment in the photoautotrophic cyanobacterium, Synechococcus sp. PCC 7002. This method enables the identification of redox changes in as little as 30 seconds after nutrient perturbation, and oscillations in reduction and oxidation for 60 minutes following the perturbation. The redox changes were validated by demonstrating that protein abundances did not change per global proteomic analyses. Peptides identified by MS for global and probe-labeled samples were required to be at least six amino acids in length having a mass spectra generating function score of <=1E-10, which corresponds to an FDR of <1%. Additionally, only peptides unique in identifying a single protein were utilized to estimate protein abundances, and proteins represented by <2 unique peptides were removed. This resulted in the identification of 176 redox probe labeled protein identifications, and 808 protein identifications in the global data.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Synechococcus Sp. (strain Atcc 27264 / Pcc 7002 / Pr-6) (agmenellum Quadruplicatum)

TISSUE(S): Culture Condition:-induced Cell

SUBMITTER: Matthew Monroe

LAB HEAD: Aaron T. Wright

PROVIDER: PXD000329 | Pride | 2015-08-24

REPOSITORIES: Pride

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			Action	DRS
	NS_7002_BR_12m_1_9Feb12_Doc_11-12-19.mgf	Mgf
	NS_7002_BR_12m_1_9Feb12_Doc_11-12-19.pride.mgf.gz	Mgf
	NS_7002_BR_12m_1_9Feb12_Doc_11-12-19.raw	Raw
	NS_7002_BR_12m_1_9Feb12_Doc_11-12-19_msgfplus.mzid.gz	Mzid
	NS_7002_BR_12m_1_9Feb12_Doc_11-12-19_msgfplus.pride.mztab.gz	Mztab

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Live cell chemical profiling of temporal redox dynamics in a photoautotrophic cyanobacterium.

Sadler Natalie C NC Melnicki Matthew R MR Serres Margrethe H MH Merkley Eric D ED Chrisler William B WB Hill Eric A EA Romine Margaret F MF Kim Sangtae S Zink Erika M EM Datta Suchitra S Smith Richard D RD Beliaev Alexander S AS Konopka Allan A Wright Aaron T AT

ACS chemical biology 20131106 1

Protein reduction-oxidation (redox) modification is an important mechanism that allows microorganisms to sense environmental changes and initiate cellular responses. We have developed a quantitative chemical probe approach for live cell labeling and imaging of proteins that are sensitive to redox modifications. We utilize this in vivo strategy to identify 176 proteins undergoing ∼5-10-fold dynamic redox change in response to nutrient limitation and subsequent replenishment in the photoautotrophi ...[more]

PMID: 24168666

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