Cloning and sequencing a putative pyrophosphate-dependent phosphofructokinase gene from Entamoeba histolytica

Huang, Min; Albach, Richard A.; Chang, Kwang-Poo; Tripathi, Rakesh; Kemp, Robert G.

doi:10.1016/0167-4781(94)00216-p

Cited by 14 publications

(12 citation statements)

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“…Further, it does not appear likely that the E. histolytica, G. lamblia, and T. vaginalis FD came from the same bacterium, unless that bacterium had multiple FD genes as has been described for Rhodobacter capsulatus (six) (42). Nor does it appear likely that the E. histolytica POR, ADHE, and PPFK genes came from the same bacterium as those of G. lamblia, unless the bacterium had multiple POR, ADHE, and PPFK genes, and different fermentation genes were lost from E. histolytica and G. lamblia (3,26,48).…”

Section: Discussionmentioning

confidence: 97%

“…(iii) E. histolytica appears to have numerous other bacterial genes, including those that encode two PP i -dependent glycolytic enzymes, HSP60, NNT, SOD, disulfide oxidoreductases, and possibly glyceraldehyde-3-phosphate dehydrogenase (8,10,13,26,50,55,68).…”

Section: Discussionmentioning

confidence: 99%

“…Note that it is also possible that the E. histolytica genes were acquired via bacterial plasmids or transposons rather than by a bacterial endosymbiont. (8,9,25,26,31,44,45,64). Positional identities of each enzyme with those of the most similar bacterium are shown in parentheses.…”

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confidence: 99%

“…also appears to be derived by horizontal transfer from bacteria (50,55). Fifth, E. histolytica contains two bacterium-like pyrophosphate (PP i )-dependent glycolytic enzymes, a phosphofructokinase (PPFK) and pyruvate phosphate dikinase, which substitute for ATP-dependent glycolytic enzymes present in most other eubacteria and eukaryotes (3,8,26). Sixth, another amitochondriate protozoan parasite, Trichomonas vaginalis, appears to contain genes derived from a bacterial endosymbiont ( Fig.…”

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confidence: 99%

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Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica

Rosenthal¹,

Mai²,

Caplivski³

et al. 1997

J Bacteriol

103

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Entamoeba histolytica is an amitochondriate protozoan parasite with numerous bacterium-like fermentation enzymes including the pyruvate:ferredoxin oxidoreductase (POR), ferredoxin (FD), and alcohol dehydrogenase E (ADHE). The goal of this study was to determine whether the genes encoding these cytosolic E. histolytica fermentation enzymes might derive from a bacterium by horizontal transfer, as has previously been suggested for E. histolytica genes encoding heat shock protein 60, nicotinamide nucleotide transhydrogenase, and superoxide dismutase. In this study, the E. histolytica por gene and the adhE gene of a second amitochondriate protozoan parasite, Giardia lamblia, were sequenced, and their phylogenetic positions were estimated in relation to POR, ADHE, and FD cloned from eukaryotic and eubacterial organisms. The E. histolytica por gene encodes a 1,620-amino-acid peptide that contained conserved iron-sulfur-and thiamine pyrophosphate-binding sites. The predicted E. histolytica POR showed fewer positional identities to the POR of G. lamblia (34%) than to the POR of the enterobacterium Klebsiella pneumoniae (49%), the cyanobacterium Anabaena sp. (44%), and the protozoan Trichomonas vaginalis (46%), which targets its POR to anaerobic organelles called hydrogenosomes. Maximum-likelihood, neighbor-joining, and parsimony analyses also suggested as less likely E. histolytica POR sharing more recent common ancestry with G. lamblia POR than with POR of bacteria and the T. vaginalis hydrogenosome. The G. lamblia adhE encodes an 888-amino-acid fusion peptide with an aldehyde dehydrogenase at its amino half and an iron-dependent (class 3) ADH at its carboxy half. The predicted G. lamblia ADHE showed extensive positional identities to ADHE of Escherichia coli (49%), Clostridium acetobutylicum (44%), and E. histolytica (43%) and lesser identities to the class 3 ADH of eubacteria and yeast (19 to 36%). Phylogenetic analyses inferred a closer relationship of the E. histolytica ADHE to bacterial ADHE than to the G. lamblia ADHE. The 6-kDa FD of E. histolytica and G. lamblia were most similar to those of the archaebacterium Methanosarcina barkeri and the ␦-purple bacterium Desulfovibrio desulfuricans, respectively, while the 12-kDa FD of the T. vaginalis hydrogenosome was most similar to the 12-kDa FD of ␥-purple bacterium Pseudomonas putida. E. histolytica genes (and probably G. lamblia genes) encoding fermentation enzymes therefore likely derive from bacteria by horizontal transfer, although it is not clear from which bacteria these amebic genes derive. These are the first nonorganellar fermentation enzymes of eukaryotes implicated to have derived from bacteria.The endosymbiont hypothesis or serial endosymbiosis theory, one of the most exciting ideas in evolutionary biology, postulates that the mitochondria and chloroplasts of eukaryotic cells derive from an endocytosed ␣-purple bacterium and cyanobacterium, respectively ( Fig. 1) (18,19,35,63). Although bacterial rRNA genes as well as those encoding some structural protei...

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica

Rosenthal¹,

Mai²,

Caplivski³

et al. 1997

J Bacteriol

103

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“…Interestingly, the simplest PFK proteins, PP i -dependent homodimeric enzymes lacking allosteric control, are encountered in P. freudenreichii (28), Giardia lamblia (32), and Entamoeba histolytica (26), which have an obligate anaerobic metabolism. The last two species are considered to have branched off from the eukaryotic lineage before Eucarya acquired mitochondria (33).…”

Section: Discussionmentioning

confidence: 99%

Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase

et al. 1996

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The actinomycete Amycolatopsis methanolica is one of the few known gram-positive bacteria which can use methanol as a growth substrate (14). Until recently, research on A. methanolica focused on methanol metabolism (2) and on regulation of aromatic-amino-acid biosynthesis (16,17). It was shown previously that A. methanolica metabolizes glucose via the EmbdenMeyerhof-Parnas pathway (2).In most organisms, the glycolytic flux is controlled at the level of phosphofructokinase (PFK) (44), which catalyzes the irreversible ATP-dependent phosphorylation of fructose-6-phosphate (EC 2.7.1.11). The ATP-dependent PFKs (ATPPFKs) are allosterically regulated, have a high K m for their substrate fructose-6-phosphate, and a neutral pH optimum. Three classes can be recognized. The bacterial enzyme has a tetrameric structure of identical subunits each with a molecular mass of 35 kDa and is allosterically regulated by phosphoenolpyruvate and ADP (44). Like the bacterial enzyme, the mammalian enzyme is composed of four identical subunits, although the subunits are substantially larger (85 kDa). The yeast enzyme is an octamer composed of two nonidentical subunits with molecular masses of 112 and 118 kDa. Sequence comparisons among the three classes of ATP-PFK proteins indicate that the yeast and mammalian enzymes have arisen as a result of gene duplication and fusion events. The activities of the yeast and mammalian enzymes are generally regulated by citrate, ATP, and fructose-2,6-bisphosphate (20, 44).In some bacteria, plants, and protozoa, a PP i -dependent PFK (PP i -PFK) (EC 2.7.1.90) is encountered (33). In contrast to the ATP-PFK, the PP i -dependent enzyme catalyzes the reversible phosphorylation of fructose-6-phosphate (36). A correlation between anaerobic metabolism and the presence of PP i -PFK has led to the suggestion that this enzyme is better adapted to anaerobiosis than its ATP-dependent counterpart is. In Propionibacterium freudenreichii and a number of protists, a homodimeric PP i -PFK that is not allosterically regulated is present (33,35). This class of PP i -PFK is characterized by a low K m for fructose-6-phosphate and an acidic pH optimum for the phosphorylation of fructose-6-phosphate. In plants, PP i -PFK is present as a heterotetrameric enzyme composed of two nonidentical subunits with molecular masses of 60 and 65 kDa (3). As with the yeast and mammalian enzymes, the activity of the plant PP i -PFK is regulated by fructose-2,6-bisphosphate, the K m for fructose-6-phosphate is high, and the enzyme has a neutral pH optimum for the glycolytic reaction.We have previously purified and characterized the PP i -PFK of A. methanolica (2). As is typical for PP i -PFK enzymes, the enzyme activity was not allosterically regulated and catalyzed the reversible phosphorylation of fructose-6-phosphate. However, the A. methanolica PFK has a number of biochemical characteristics in common with the bacterial ATP-dependent enzymes: it is a tetramer of identical subunits, the K m for fructose-6-phosphate is high, and it has a n...

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Amebiasis:Entamoeba HistolyticaInfections

Martı́nez-Palomo¹,

Espinosa‐Cantellano²

2010

Topley &Amp; Wilson's Microbiology and Microbial Infections

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Cloning and sequencing a putative pyrophosphate-dependent phosphofructokinase gene from Entamoeba histolytica

Cited by 14 publications

References 11 publications

Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica

Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica

Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase

Amebiasis:Entamoeba HistolyticaInfections

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