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Aldehyde dehydrogenase in tobacco pollen

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Abstract

Acetaldehyde is one of the intermediate products of ethanolic fermentation, which can be reduced to ethanol by alcohol dehydrogenase (ADH). Alternatively, acetaldehyde can be oxidized to acetate by aldehyde dehydrogenase (ALDH) and subsequently converted to acetyl-CoA by acetyl-CoA synthetase (ACS). To study the expression of ALDHs in plants we isolated and characterized a cDNA coding for a putative mitochondrial ALDH (TobAldh2A) in Nicotiana tabacum/. TobALDH2A shows 54–60% identity at the amino acid level with other ALDHs and shows 76% identity with maize Rf2, a gene involved in restoration of male fertility in cms-T maize. TobAldh2A transcripts and protein were present at high levels in the male and female reproductive tissues. Expression in vegetative tissues was much lower and no induction by anaerobic incubation was observed. This suggests that TobALDH expression is not part of the anaerobic response, but may have another function. The use of specific inhibitors of ALDH and the pyruvate dehydrogenase (PDH) complex indicates that ALDH activity is important for pollen tube growth, and thus may have a function in biosynthesis or energy production.

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Authors and Affiliations

  1. Institute of Plant Physiology, University of Berne, Altenbergrain 21, 3013, Berne, Switzerland

    Roel G.L. op den Camp & Cris Kuhlemeier*

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  1. Roel G.L. op den Camp
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  2. Cris Kuhlemeier*
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op den Camp, R.G., Kuhlemeier*, C. Aldehyde dehydrogenase in tobacco pollen. Plant Mol Biol 35, 355–365 (1997). https://doi.org/10.1023/A:1005889129491

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