December 1, 2014
Journal Article

Proteome-wide Light/Dark Modulation of Thiol Oxidation in Cyanobacteria Revealed by Quantitative Site-Specific Redox Proteomics

Abstract

Reversible protein thiol oxidation is an essential regulatory mechanism of photosynthesis, metabolism, and gene expression in photosynthetic organisms. Herein, we present the first proteome-wide quantitative site-specific profiling of in vivo dynamics of thiol oxidation modulated by light/dark in cyanobacterium Synechocystis sp. PCC 6803, an oxygenic photosynthetic prokaryote. Our proteomic approach integrates resin-assisted enrichment with isobaric labeling to enable site-specific and quantitative measurements of reversibly oxidized thiols. The redox dynamics of ~2,200 cysteine sites from 1,060 proteins under different conditions (light, dark, and in the presence of a photosystem II inhibitor DCMU) were quantified. The results revealed broad proteome-wide changes in thiol oxidation in many key biological processes including photosynthesis, carbon fixation, and glycolysis. Moreover, the redox sensitivity data provides a good prediction of potential functional cysteine sites for proteins of interest. Together, our findings provided significant novel insights into the broad redox regulation of photosynthetic organisms.

Revised: July 22, 2020 | Published: December 1, 2014

Citation

Guo J., A.Y. Nguyen, Z. Dai, D. Su, M.J. Gaffrey, R.J. Moore, and J.M. Jacobs, et al. 2014. Proteome-wide Light/Dark Modulation of Thiol Oxidation in Cyanobacteria Revealed by Quantitative Site-Specific Redox Proteomics. Molecular & Cellular Proteomics 13, no. 12:3270-3285. PNNL-SA-100244. doi:10.1074/mcp.M114.041160