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D -Lactate is oxidized by two classes of  D -lactate dehydrogenase ( D -LDH), namely, NAD-dependent and NAD-independent  D -LDHs. Little is known about the characteristics and biological functions of  D -LDHs in rice. In this study, a functional NAD-independent  D -LDH (LOC_Os07g06890) was identified in rice, as a result of alternative splicing events. Characterization of the expression profile, subcellular localization, and enzymatic properties of the functional Os D -LDH revealed that it is a mitochondrial cytochrome- c -dependent  D -LDH with high affinity and catalytic efficiency. Functional analysis of  Os D -LDH  RNAi transgenic rice demonstrated that Os D -LDH participates in methylglyoxal metabolism by affecting the activity of the glyoxalase system and aldo-keto reductases. Under methylglyoxal treatment, silencing of Os D -LDH in rice resulted in the accumulation of methylglyoxal and  D -lactate, the decrease of reduced glutathione in leaves, and ultimately severe growth inhibition. Moreover, the detached leaves of  Os D -LDH  RNAi plants were more sensitive to salt stress. However, the silencing of Os D -LDH did not affect the growth under photorespiration conditions. Our results provide new insights into the role of NAD-independent  D -LDHs in rice.

Silencing of D-Lactate Dehydrogenase Impedes Glyoxalase System and Leads to Methylglyoxal Accumulation and Growth Inhibition in Rice