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


ABSTRACT: 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 OsD-LDH revealed that it is a mitochondrial cytochrome-c-dependent D-LDH with high affinity and catalytic efficiency. Functional analysis of OsD-LDH RNAi transgenic rice demonstrated that OsD-LDH participates in methylglyoxal metabolism by affecting the activity of the glyoxalase system and aldo-keto reductases. Under methylglyoxal treatment, silencing of OsD-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 OsD-LDH RNAi plants were more sensitive to salt stress. However, the silencing of OsD-LDH did not affect the growth under photorespiration conditions. Our results provide new insights into the role of NAD-independent D-LDHs in rice.

SUBMITTER: An B 

PROVIDER: S-EPMC5723347 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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

An Baoguang B   Lan Jie J   Deng Xiaolong X   Chen Silan S   Ouyang Chao C   Shi Huiyun H   Yang Jing J   Li Yangsheng Y  

Frontiers in plant science 20171205


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 OsD-LDH revealed that it is a mitochondrial  ...[more]

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