The roles of aldehyde dehydrogenases (ALDHs) in the PDH bypass of Arabidopsis
1 Department of Genetics, Development and Cell Biology, Iowa State University, Ames, Iowa 50011, USA
2 Interdepartmental Genetics Program, Iowa State University, Ames, Iowa 50011, USA
3 Department of Agronomy, Iowa State University, Ames, Iowa 50011, USA
4 Center for Plant Genomics, Iowa State University, Ames, Iowa 50011, USA
5 Current address : Center for Applied Genetic Technologies, University of Georgia, Athens, GA 30602, USA
BMC Biochemistry 2009, 10:7 doi:10.1186/1471-2091-10-7Published: 25 March 2009
Eukaryotic aldehyde dehydrogenases (ALDHs, EC 1.2.1), which oxidize aldehydes into carboxylic acids, have been classified into more than 20 families. In mammals, Family 2 ALDHs detoxify acetaldehyde. It has been hypothesized that plant Family 2 ALDHs oxidize acetaldehyde generated via ethanolic fermentation, producing acetate for acetyl-CoA biosynthesis via acetyl-CoA synthetase (ACS), similar to the yeast pathway termed the "pyruvate dehydrogenase (PDH) bypass". Evidence for this pathway in plants has been obtained from pollen.
To test for the presence of the PDH bypass in the sporophytic tissue of plants, Arabidopsis plants homozygous for mutant alleles of all three Family 2 ALDH genes were fed with 14C-ethanol along with wild type controls. Comparisons of the incorporation rates of 14C-ethanol into fatty acids in mutants and wild type controls provided direct evidence for the presence of the PDH bypass in sporophytic tissue. Among the three Family 2 ALDHs, one of the two mitochondrial ALDHs (ALDH2B4) appears to be the primary contributor to this pathway. Surprisingly, single, double and triple ALDH mutants of Arabidopsis did not exhibit detectable phenotypes, even though a Family 2 ALDH gene is required for normal anther development in maize.
The PDH bypass is active in sporophytic tissue of plants. Blocking this pathway via triple ALDH mutants does not uncover obvious visible phenotypes.