Thiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms,and thioredoxin plays a key role by controlling the thiol-disulfide status of target proteins.Recent redox proteomic studies revealed hundreds of proteins regulated by glutathionylation and nitrosylation in the unicellular green alga Chlamydomonas reinhardtii,while much less is known about the thioredoxin interactome in this organism.By combining qualitative and quantitative proteomic analyses,we have comprehensively investigated the Chlamydomonas thioredoxome and 1188 targets have been identified.They participate in a wide range of metabolic pathways and cellular processes.This study broadens not only the redox regulation to new enzymes involved in well-known thioredoxin-regulated metabolic pathways but also sheds light on cellular processes for which data supporting redox regulation are scarce (aromatic amino acid biosynthesis,nuclear transport,etc),Moreover,we characterized 1052 thioredoxin-dependent regulatory sites and showed that these data constitute a valuable resource for future functional studies in Chlamydomonas.By comparing this thioredoxome with proteomic data for glutathionylation and nitrosylation at the protein and cysteine levels,this work confirms the existence of a complex redox regulation network in Chlamydomonas and provides evidence of a tremendous selectivity of redox post-translational modifications for specific cysteine residues.