July 22, 2020
Journal Article

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

Himadri Pakrasi
Weijun Qian
Ziyu Dai
Dian Su
Jon Jacobs
Jia Guo
Amelia Nguyen

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. MCP 13, no. 12:3270-3285. PNNL-SA-100244. doi:10.1074/mcp.M114.041160