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A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis

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Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), localized in the cytosol of Trichomonas vaginalis, was partially purified. The enzyme is specific for NAD+ and is similar in most of its catalytic properties to glycolytic GAPDHs from other organisms. Its sensitivity to koningic acid is similar to levels observed in GAPDHs from eubacteria and two orders of magnitude lower than those observed for eukaryotic GAPDHs. The complete amino acid sequence of T. vaginalis GAPDH was derived from the N-terminal sequence of the purified protein and the deduced sequence of a cDNA clone. It showed great similarity to other eubacterial and eukaryotic GAPDH sequences. The sequence of the S-loop displayed a eubacterial signature. The overall sequence was more similar to eubacterial sequences than to cytosolic and glycosomal eukaryotic sequences. In phylogenetic trees obtained with distance matrix and parsimony methods T. vaginalis GAPDH clustered with its eubacterial homologs. GAPDHs of other amitochondriate protists, belonging to early branches of the eukaryotic lineage (Giardia lamblia and Entamoeba histolytica—Smith M.W. and Doolittle R.F., unpublished data in GenBank), showed typical eukaryotic signatures and clustered with other eukaryotic sequences, indicating that T. vaginalis GAPDH occupies an anomalous position, possibly due to horizontal gene transfer from a eubacterium.

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  1. Anton Markoš

    Present address: Department of Physiology and Developmental Biology, Charles University, 128 44 Prague 2, Vinična 7, Czech Republic

  2. Anya Miretsky

    Present address: Department of Medical Psychology, Uniformed Services University of the Health Sciences, 20814, Bethesda, MD, USA

Authors and Affiliations

  1. The Rockefeller University, 1230 York Avenue, 10021, New York, NY, USA

    Anton Markoš, Anya Miretsky & Miklós Müller

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  1. Anton Markoš
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Correspondence to: M. Müller

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Markoš, A., Miretsky, A. & Müller, M. A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis . J Mol Evol 37, 631–643 (1993). https://doi.org/10.1007/BF00182749

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