Fecha de publicación: -- Fuente: PubMed "rice" Phytochemistry. 2026 Sep 24:115092. doi: 10.1016/j.phytochem.2026.115092. Online ahead of print.ABSTRACTCytosolic detoxification through vacuolar sequestration is essential for plant growth and stress tolerance. A key driver of this process is the vacuolar ABC transporter, ABCC1, which sequesters diverse amphiphilic anions including glutathione (GS)-conjugates, glucuronic acid-conjugates, and thiol-coordinated metal complexes. However, mechanistic studies of plant ABCC1 have largely relied on Arabidopsis genetics and crude membrane transport assays. Here, phylogenetic and sequence-guided analysis of ABCC1 orthologs from multiple plant species was combined with in vitro functional assays with purified protein to investigate plant ABCC1 transporter activity. Compared to mammalian ABCC1, all plant ABCC1 orthologs contain a conserved bipartite binding pocket with a cationic pocket for anion recognition and a hydrophobic pocket. Key differences between mammalian and plant ABCC1 include a substitution in the cation coordinating histidine residue that is compensated by a peripheral arginine mutation to preserve the cationic electrostatic environment. Furthermore, the plant ABCC1 hydrophobic pocket is enlarged relative to its mammalian counterpart due to several substitutions with smaller side-chain residues. To investigate the in vitro activity of plant ABCC1, several orthologs were screened for expression, and those from maize, date palm, and rice exhibited high biochemical stability and comparable substrate-stimulated ATPase activity. ZmABCC1 was further characterized through a series of assay optimization experiments, which found that its ATPase activity is strongly stimulated by E217βG and GS-conjugates, and inhibited by orthovanadate. This study verifies that ABCC1 is widely conserved across plant species with a consistent substrate binding pocket and activity, supporting its role in cytosolic detoxification in plants.PMID:42785454 | DOI:10.1016/j.phytochem.2026.115092