Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates

ABSTRACT. Complete nucleotide sequences have been established for two genes ( gap1 and gap2 ) coding for glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH, EC 1.2.1.12) homologs in the diplomonad Giardia lamblia. In addition, almost complete sequences of the GAPDH open reading frames were obtained fro...

Full description

Bibliographic Details
Published in:Journal of Eukaryotic Microbiology
Main Authors: ROZARIO, CATHERINE, MORIN, LOÏC, ROGER, ANDREW J., SMITH, MICHAEL W., MÜLLER, MIKLÓS
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 1996
Subjects:
Online Access:http://dx.doi.org/10.1111/j.1550-7408.1996.tb03997.x
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1550-7408.1996.tb03997.x
https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1550-7408.1996.tb03997.x
id crwiley:10.1111/j.1550-7408.1996.tb03997.x
record_format openpolar
spelling crwiley:10.1111/j.1550-7408.1996.tb03997.x 2024-06-02T08:03:43+00:00 Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates ROZARIO, CATHERINE MORIN, LOÏC ROGER, ANDREW J. SMITH, MICHAEL W. MÜLLER, MIKLÓS 1996 http://dx.doi.org/10.1111/j.1550-7408.1996.tb03997.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1550-7408.1996.tb03997.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1550-7408.1996.tb03997.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of Eukaryotic Microbiology volume 43, issue 4, page 330-340 ISSN 1066-5234 1550-7408 journal-article 1996 crwiley https://doi.org/10.1111/j.1550-7408.1996.tb03997.x 2024-05-03T12:06:06Z ABSTRACT. Complete nucleotide sequences have been established for two genes ( gap1 and gap2 ) coding for glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH, EC 1.2.1.12) homologs in the diplomonad Giardia lamblia. In addition, almost complete sequences of the GAPDH open reading frames were obtained from PCR products for two free‐living diplomonad species, Trepomonas agilis and Hexamita inflata , and a parasite of Atlantic salmon, an as yet unnamed species with morphological affinities to Spironucleus. Giardia lamblia gap 1 and the genes from the three other diplomonad species show high similarity to each other and to other glycolytic GAPDH genes. All amino‐acyl residues known to be highly conserved in this enzyme are also conserved in these sequences. Giardia lamblia gap2 gene is more divergent and its putative translation reveals the presence of a cysteine and serine‐rich insertion resembling a metal binding finger. This motif has not yet been noted in other GAPDH molecules. All sequences contain an S‐loop signature with characteristics close to those of eukaryotes. In phylogenetic reconstructions based on the derived amino acid sequences with neighborjoining, parsimony and maximum‐likelihood methods the four typical GAPDH sequences of diplomonads cluster into a single clade. Within this clade, G. lamblia gap1 shares a common ancestor with the rest of the genes. The latter are more closely related to each other, indicating an early separation of the lineage leading to the genus Giardia from the lineage encompassing the morphologically less differentiated genera, Trepomonas, Hexamita and that of the unnamed species. This result is discordant with the orthogonal evolution of diplomonads suggested on the basis of comparative morphology. In neighbor‐joining reconstructions G. lamblia gap2 occupies a variable position, due to its great divergence. In parsimony and maximum likelihood analysis however, it shares a most recent common ancestor with the typical G. lamblia gap1 gene, suggesting that it diverged after the ... Article in Journal/Newspaper Atlantic salmon Wiley Online Library Journal of Eukaryotic Microbiology 43 4 330 340
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description ABSTRACT. Complete nucleotide sequences have been established for two genes ( gap1 and gap2 ) coding for glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH, EC 1.2.1.12) homologs in the diplomonad Giardia lamblia. In addition, almost complete sequences of the GAPDH open reading frames were obtained from PCR products for two free‐living diplomonad species, Trepomonas agilis and Hexamita inflata , and a parasite of Atlantic salmon, an as yet unnamed species with morphological affinities to Spironucleus. Giardia lamblia gap 1 and the genes from the three other diplomonad species show high similarity to each other and to other glycolytic GAPDH genes. All amino‐acyl residues known to be highly conserved in this enzyme are also conserved in these sequences. Giardia lamblia gap2 gene is more divergent and its putative translation reveals the presence of a cysteine and serine‐rich insertion resembling a metal binding finger. This motif has not yet been noted in other GAPDH molecules. All sequences contain an S‐loop signature with characteristics close to those of eukaryotes. In phylogenetic reconstructions based on the derived amino acid sequences with neighborjoining, parsimony and maximum‐likelihood methods the four typical GAPDH sequences of diplomonads cluster into a single clade. Within this clade, G. lamblia gap1 shares a common ancestor with the rest of the genes. The latter are more closely related to each other, indicating an early separation of the lineage leading to the genus Giardia from the lineage encompassing the morphologically less differentiated genera, Trepomonas, Hexamita and that of the unnamed species. This result is discordant with the orthogonal evolution of diplomonads suggested on the basis of comparative morphology. In neighbor‐joining reconstructions G. lamblia gap2 occupies a variable position, due to its great divergence. In parsimony and maximum likelihood analysis however, it shares a most recent common ancestor with the typical G. lamblia gap1 gene, suggesting that it diverged after the ...
format Article in Journal/Newspaper
author ROZARIO, CATHERINE
MORIN, LOÏC
ROGER, ANDREW J.
SMITH, MICHAEL W.
MÜLLER, MIKLÓS
spellingShingle ROZARIO, CATHERINE
MORIN, LOÏC
ROGER, ANDREW J.
SMITH, MICHAEL W.
MÜLLER, MIKLÓS
Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates
author_facet ROZARIO, CATHERINE
MORIN, LOÏC
ROGER, ANDREW J.
SMITH, MICHAEL W.
MÜLLER, MIKLÓS
author_sort ROZARIO, CATHERINE
title Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates
title_short Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates
title_full Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates
title_fullStr Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates
title_full_unstemmed Primary Structure and Phylogenetic Relationships of Glyceraldehyde‐3‐Phosphate Dehydrogenase Genes of Free‐Living and Parasitic Diplomonad Flagellates
title_sort primary structure and phylogenetic relationships of glyceraldehyde‐3‐phosphate dehydrogenase genes of free‐living and parasitic diplomonad flagellates
publisher Wiley
publishDate 1996
url http://dx.doi.org/10.1111/j.1550-7408.1996.tb03997.x
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1550-7408.1996.tb03997.x
https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1550-7408.1996.tb03997.x
genre Atlantic salmon
genre_facet Atlantic salmon
op_source Journal of Eukaryotic Microbiology
volume 43, issue 4, page 330-340
ISSN 1066-5234 1550-7408
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1111/j.1550-7408.1996.tb03997.x
container_title Journal of Eukaryotic Microbiology
container_volume 43
container_issue 4
container_start_page 330
op_container_end_page 340
_version_ 1800748324553228288