Isolation and developmental expression analysis of L-myo-inositol-1-phosphate synthase in four Actinidia species

Myo-inositol (MI) is an important polyol involved in cellular signal transduction, auxin storage, osmotic regulation, and membrane formation. It also serves as a precursor for the production of pinitol, ascorbic acid, and members of the raffinose family. The first committed step for MI formation is catalyzed by L-myo-inositol-1-phosphate synthase (MIPS). We isolated MIPS cDNA sequences from Actinidia eriantha, Actinidia rufa, and Actinidia arguta and compared them with that of Actinidia deliciosa. Each comprised 1533 bp, encoding 510 amino acids with a predicted molecular weight of 56.5 KDa. The MIPS protein was highly conserved in Actinidia, sharing 98.94% identity among species. The MIPS gene was expressed in the flowers, leaves, petioles, and carpopodia. Similarly high levels of expression were detected in the young fruit of all four species. Overall activity of the enzyme was also maximal in young fruit, indicating that this developmental stage is the key point for MI synthesis in Actinidia. Among the four species, A. arguta had the greatest concentration of MI as well as the highest ratios of MI:sucrose and MI:glucose+fructose. This suggests that conversion to MI from carbohydrates was most efficient in A. arguta during early fruit development.