The roles of aldehyde dehydrogenases ALDHs in the PDH bypass of ArabidopsisReportar como inadecuado

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BMC Biochemistry

, 10:7

First Online: 25 March 2009Received: 12 August 2008Accepted: 25 March 2009


BackgroundEukaryotic 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.

ResultsTo 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 C-ethanol along with wild type controls. Comparisons of the incorporation rates of C-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.

ConclusionThe PDH bypass is active in sporophytic tissue of plants. Blocking this pathway via triple ALDH mutants does not uncover obvious visible phenotypes.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2091-10-7 contains supplementary material, which is available to authorized users.

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Autor: Yanling Wei - Ming Lin - David J Oliver - Patrick S Schnable


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