Chemical inhibition of the target of rapamycin kinase in Chlamydomonas reinhardtii leads to rapid cysteine oxidation and sustained physiological changes.

The target of rapamycin (TOR) kinase is a key metabolic regulator with a role in diverse processes, including nutritional sensing, protein translation, and autophagy. In the green alga Chlamydomonas reinhardtii, TOR maintains these responsibilities and is additionally linked to the regulation of increased triacylglycerol accumulation. In this study, we used an ATP-competitive inhibitor (AZD8055) to inactivate TOR kinase in vivo and quantified any accompanying changes in global protein abundance and reversible cysteine oxidation.