Primary sequence of a putative pyrophosphate-linked phosphofructokinase gene of Giardia lamblia

Rozario, Catherine; Smith, Michael W.; Müller, Miklós

doi:10.1016/0167-4781(94)00217-q

Cited by 18 publications

(14 citation statements)

References 19 publications

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“…The alignment proposed was robust in certain parts and less so in others. The data are in agreement with the notion repeatedly stressed that the amino-terminal half of the molecule, through the MGR tripeptide (residues 194-196 in T. vaginalis), is more conserved than the carboxyterminal half (Ladror et al 1991;Rozario et al 1995). The increasing number of related sequences available made the alignment of the carboxy-terminal half of the divergent PFK sequences easier than in the past.…”

Section: Alignment Of Pfk Sequences From Various Organismssupporting

confidence: 80%

“…However, they show an unexpectedly high level of divergence in their size and subunit structure. Sequences determined recently from several protists (Rozario et al 1995;Huang et al 1995;Wessberg et al 1995;Bruchhaus et al 1996;Michels et al 1997;Deng et al 1998) and compared with new data for several eubacteria confirm this high diversity and raise interesting questions concerning the evolutionary history of the homomeric PFKs.…”

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confidence: 91%

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The Pyrophosphate-Dependent Phosphofructokinase of the Protist, Trichomonas vaginalis, and the Evolutionary Relationships of Protist Phosphofructokinases

et al. 1998

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The pyrophosphate-dependent phosphofructokinase (PPi-PFK) of the amitochondriate protist Trichomonas vaginalis has been purified. The enzyme is a homotetramer of about 50 kDa subunits and is not subject to allosteric regulation. The protein was fragmented and a number of peptides were sequenced. Based on this information a PCR product was obtained from T. vaginalis gDNA and used to isolate corresponding cDNA and gDNA clones. Southern analysis indicated the presence of five genes. One open reading frame (ORF) was completely sequenced and for two others the 5' half of the gene was determined. The sequences were highly similar. The complete ORF corresponded to a polypeptide of about 46 kDa. All the peptide sequences obtained were present in the derived sequences. The complete ORF was highly similar to that of other PFKs, primarily in its amino-terminal half. The T. vaginalis enzyme was most similar to PPi-PFK of the mitochondriate heterolobosean, Naegleria fowleri. Most of the residues shown or assumed to be involved in substrate binding in other PPi-PFKs were conserved in the T. vaginalis enzyme. Direct comparison and phylogenetic reconstruction revealed a significant divergence among PPi-PFKs and related enzymes, which can be assigned to at least four distantly related groups, three of which contain enzymes of protists. The separation of these groups is supported with a high percentage of bootstrap proportions. The short T. vaginalis PFK shares a most recent common ancestor with the enzyme from N. fowleri. This pair is clearly separated from a group comprising the long (>60-kDa) enzymes from Giardia lamblia, Entamoeba histolytica pfk2, the spirochaetes Borrelia burgdorferi and Trepomena pallidum, as well as the alpha- and beta-subunits of plant PPi-PFKs. The third group ("X") containing protist sequences includes the glycosomal ATP-PFK of Trypanosoma brucei, E. histolytica pfk1, and a second sequence from B. burgdorferi. The fourth group ("Y") comprises cyanobacterial and high-G + C, Gram-positive eubacterial sequences. The well-studied PPi-PFK of Propionibacterium freudenreichii is highly divergent and cannot be assigned to any of these groups. These four groups are well separated from typical ATP-PFKs, the phylogenetic analysis of which confirmed relationships established earlier. These findings indicate a complex history of a key step of glycolysis in protists with several early gene duplications and possible horizontal gene transfers.

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Section: Alignment Of Pfk Sequences From Various Organismssupporting

confidence: 80%

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confidence: 91%

The Pyrophosphate-Dependent Phosphofructokinase of the Protist, Trichomonas vaginalis, and the Evolutionary Relationships of Protist Phosphofructokinases

et al. 1998

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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: 98%

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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“…The flagellated trophozoite form lives attached to the intestinal mucous of its host and differentiates into highly infectious cyst forms which are excreted in the feces. In addition to the particular features of having two nuclei, lack of mitochondria and normal endoplasmic reticulum or Golgi system, reviewed by Gillin (3), it has an important evolutionary position, being basal to all eukaryotes with mitochondria in phylogenies inferred from small subunit rRNAs (4) and coding genes (5,6). Nevertheless, recent reports suggest that diplomonads are secondarily amitochondriate (7,8).…”

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confidence: 97%

Trends of Amino Acid Usage in the Proteins from the Unicellular Parasite Giardia lamblia

Garat

Musto

2000

Biochemical and Biophysical Research Communications

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Primary sequence of a putative pyrophosphate-linked phosphofructokinase gene of Giardia lamblia

Cited by 18 publications

References 19 publications

The Pyrophosphate-Dependent Phosphofructokinase of the Protist, Trichomonas vaginalis, and the Evolutionary Relationships of Protist Phosphofructokinases

The Pyrophosphate-Dependent Phosphofructokinase of the Protist, Trichomonas vaginalis, and the Evolutionary Relationships of Protist Phosphofructokinases

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

Trends of Amino Acid Usage in the Proteins from the Unicellular Parasite Giardia lamblia

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