The aim was to determine the function of peroxisomal NAD⁺-malate dehydrogenase (PMDH) in fatty acid β-oxidation and the glyoxylate cycle in Arabidopsis. Seeds in which both PMDH genes are disrupted by T-DNA insertions germinate, but seedling establishment is dependent on exogenous sugar. Mutant seedlings mobilize their triacylglycerol very slowly and growth is insensitive to 2,4-dichlorophenoxybutyric acid. Thus mutant seedlings are severely impaired in β-oxidation, even though microarray analysis shows that β-oxidation genes are expressed normally. The mutant phenotype was complemented by expression of a cDNA encoding PMDH with either its native peroxisome targeting signal-2 (PTS2) targeting sequence or a heterologous PTS1 sequence. In contrast to the block in β-oxidation in mutant seedlings, [¹⁴C]acetate is readily metabolized into sugars and organic acids, thereby demonstrating normal activity of the glyoxylate cycle. We conclude that PMDH serves to reoxidize NADH produced from fatty acid β-oxidation and does not participate directly in the glyoxylate cycle.

Item Type:	Refereed Article
Keywords:	peroxisome, malate dehydrogenase, b-oxidation, glyoxylate cycle, fatty acids, Arabidopsis
Research Division:	Biological Sciences
Research Group:	Plant Biology
Research Field:	Plant Physiology
Objective Division:	Expanding Knowledge
Objective Group:	Expanding Knowledge
Objective Field:	Expanding Knowledge in the Biological Sciences
Author:	Smith, SM (Professor Steven Smith)
ID Code:	101509
Year Published:	2007
Web of Science® Times Cited:	74
Deposited By:	Plant Science
Deposited On:	2015-06-25
Last Modified:	2015-09-24
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