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The phosphorylation status of eucalyptus leaf proteins exposed to CO2-enriched atmosphere

Abstract

Phosphorylation is a key event in the regulation of protein activity. The reversible phosphorylation/dephosphorylation steps can modulate signaling processes, control enzymatic activity, modify sub-cellular structures and regulate gene expression. In plants, carbon dioxide is assimilated in the plant chloroplasts under a series of reactions comprising a carbon fixation step, a reduction of organic molecules phase and a regeneration of substrates multi-step phase, and is usually referred to as the Calvin-Benson (CB) cycle. The goal of the present proposal is to identify and quantitatively profile the phosphorylated forms of CB-related enzymes and other post-translationally modified proteins in Eucalyptus leaves after growth in high CO2 levels. For that, we plan to isolate, enrich and acquire large scale mass spectrometry data for all phosphopeptides contained in the leaf protein extracts. Identification and correct assignment of the post-translational modification sites will complement large-scale discovery proteomics data acquired in the same growth conditions and may be used to expand the experimental approach proposed here with the goal of monitoring the phosphorylation events in other CO2-enriched scenarios. (AU)