Oxidative stress-induced formation of covalently linked ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit dimer in tobacco plants

Abstract Objective Many abiotic stresses cause the excessive accumulation of reactive oxygen species known as oxidative stress. While analyzing the effects of oxidative stress on tobacco, we noticed the increased accumulation of a specific protein in extracts from plants treated with the oxidative-stress inducing herbicide paraquat which promotes the generation of reactive oxygen species primarily in chloroplasts. The primary objectives of this study were to identify this protein and to determine if its accumulation is indeed a result of oxidative stress. Results Here we show that the paraquat-induced protein is a covalently linked dimer of the large subunit of ribulose-1,5-bisphosphate carboxylase (LSU). Increased accumulation of this LSU dimer was also observed in tobacco plants exposed to ultra-small anatase titanium dioxide nanoparticles (nTiO2), which because of their surface reactivity cause oxidative stress by promoting the generation of superoxide anion. nTiO2 nanoparticle treatments also caused a decline in the chloroplast thylakoid proteins cytochrome f and chlorophyll a/b binding protein, thus confirming that covalent LSU dimer formation coincides with loss of chloroplast function