Legume Alternative Oxidase Isoforms Show Differential Sensitivity to Pyruvate Activation

Alternative oxidase (AOX) is an important component of the plant respiratory pathway, enabling a route for electrons that bypasses the energy-conserving, ROS-producing complexes of the mitochondrial electron transport chain. Plants contain numerous isoforms of AOX, classified as either AOX1 or AOX2. AOX1 isoforms have received the most attention due to their importance in stress responses across a wide range of species. However, the propensity for at least one isoform of AOX2 to accumulate to very high levels in photosynthetic tissues of all legumes studied to date, suggests that this isoform has specialized roles, but we know little of its properties. Previous studies with sub-mitochondrial particles of soybean cotyledons and roots indicated that differential expression of GmAOX1, GmAOX2A, and GmAOX2D across tissues might confer different activation kinetics with pyruvate. We have investigated this using recombinantly expressed isoforms of soybean AOX in a previously described bacterial system (Selinski et al., 2016, Physiologia Plantarum 157, 264-279). Pyruvate activation kinetics were similar between the two GmAOX2 isoforms but differed substantially from those of GmAOX1, suggesting that selective expression of AOX1 and 2 could determine the level of AOX activity. However, this alone cannot completely explain the differences seen in sub-mitochondrial particles isolated from different legume tissues and possible reasons for this are discussed.

Automated summary

Alternative oxidase (AOX) is an important component of the plant respiratory pathway, allowing electrons to bypass certain complexes in the mitochondrial electron transport chain. AOX has multiple isoforms, with AOX1 receiving more attention due to its importance in stress responses and AOX2 being highly accumulated in legume photosynthetic tissues. Differential activation kinetics with pyruvate were observed between AOX1 and AOX2 isoforms, suggesting that selective expression of these isoforms might determine the level of AOX activity. However, this cannot fully explain the differences seen in sub-mitochondrial particles isolated from different legume tissues.