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Phylogenetic Relationships of the Glycolytic Enzyme, Glyceraldehyde-3-Phosphate Dehydrogenase, from Parabasalid Flagellates (1998)

Viscogliosi, Eric ; Müller, Miklós

Springer

Journal of molecular evolution 47 (1998), S. 190-199

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ISSN: 1432-1432

Keywords: Key words: Amitochondriate protist — Glyceraldehyde-3-phosphate dehydrogenase — Glycolysis — Parabasala — Protein evolution —Trichomitus batrachorum— Trichomonadinae — Tritrichomonadinae

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract. Over 90% of the open reading frame of gap genes for glycolytic glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) was obtained with PCR from five species of Parabasala. With gap1 from Trichomonas vaginalis obtained earlier, the data include two sequences each for three species. All sequences were colinear with T. vaginalis gap1 and shared with it as a synapomorphy a 10- to 11-residue insertion not found in any other gap and an S-loop with characteristic features of eubacterial GAPDH. All residues known to be highly conserved in this enzyme were present. The parabasalid sequences formed a robust monophyletic group in phylogenetic reconstructions with distance-based, maximum-parsimony, and maximum-likelihood methods. The two genes of the amphibian commensal, Trichomitus batrachorum, shared a common ancestor with the rest, which separate into two well-supported lineages. T. vaginalis and Tetratrichomonas gallinarum (both representatives of Trichomonadinae) formed one, while Monocercomonas sp. and Tritrichomonas foetus formed the other. These data agreed with and/or were close to published reconstructions based on other macromolecules. They did not support the ancestral position of Monocercomonas sp. proposed on the basis of morphological characteristics but confirmed an early emergence of Trichomitus batrachorum. The sequence pairs obtained from three species indicated either gene duplications subsequent to the divergence of the corresponding lineages or a strong gene conversion later in these lineages. The parabasalid clade was a robust part of the eubacterial radiation of GAPDH and showed no relationships to the clade that contained all other eukaryotic gap genes. The data clearly reveal that the members of this lineage use in their glycolytic pathway a GAPDH species with properties and an evolutionary history that are unique among all eukaryotes studied so far.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/PL00006376

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Lysosomes in Tetrahymena pyriformis I. Some properties and lysosomal localization of acid hydrolasesSupported by grant GB-2871 from the National Science Foundation. Performed with the skillful technical assistance of Miss Magdeleine Debbaudt to whom the authors are deeply grateful. (1966)

Müller, Miklós ; Baudhuin, Pierre ; De Duve, Christian

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 68 (1966), S. 165-175

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ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: In homogenates of Tetrahymena pyriformis, five hydrolases - phosphatase, ribonuclease, deoxyribonuclease, proteinase, amylase - with acid pH optima were found. Over 75% of their activity is sedimentable with a centrifugal force of 250,000 g. min. Only 17% of the acid phosphatase and ribonuclease is active when assayed in the presence of 0.25 M sucrose at 0°. Exposure to a lowered osmotic pressure, freezing and thawing, and incubation at temperatures over 0° result in activation of the latent phosphatase and ribonuclease. After isopycnic centrifugation in a sucrose density gradient the hydrolases show a broad distribution which differs greatly from those of enzymes associated with mitochondria (succinate dehydrogenase) or with peroxisomes (catalase). The results are interpreted as evidence that the five acid hydrolases studied are localized in lysosomes which represent a distinct population of subcellular particles in Tetrahymena.

Additional Material: 5 Ill.