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Post-translational Regulation of ACO An in vitro phosphorylation assay using protein extracts of pre- and post-climacteric apple fruit and an ectopically expressed His-tagged Md ACO1 (MDP0000195885) hinted for the first time that ACO protein-protein interactions could exist (Matarasso et al., 2005), and the strongly conserved C28 as a key residue in the active site of this protease ( in silico predictions based on sequence similarity, other motifs for ACO protein-protein interactions, serine/threonine kinases, tyrosine kinases, and glycosylation were identified ( Arabidopsis ACO2 (AT1g62380) was identified as a target in a broad proteomics screen that characterized stress-induced protein S -glutathionylation, suggesting that ACO2 is post-translationally modified by glutathionylation ( Another thiol-residue modification of ACO was discovered in a large cysteine S-sulfhydration screen in Arabidopsis, which showed that ACO4 can get sulfhydrated ( 2 S production increases in stomata upon a prolonged ethylene treatment, and that this leads to the S-sulfhydration of C60 (equivalent to C63 of At ACO2) of Sl ACO1 (Solyc07g049530) and Sl ACO2 (Solyc12g005940)