Evolutionary History of Two Paralogous Glyceraldehyde 3-Phosphate Dehydrogenase Genes in Teleosts
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Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a key enzyme for carbohydrate meta-bolism in most living organisms. Recent reports and our own searches of teleost species in publicly available genomic databases have identified at least two distinct GAPDH genes in a given species. The two GAPDH genes are located on the same chromosome in teleosts, whereas they are located on the different chromosomes in mammals. Thus, we reconstructed a phy-logenetic tree to better understand the evolutionary history of the GAPDH genes in the vertebrate lineage. Our phylogenetic analysis revealed unambiguously that the two GAPDH genes of teleosts are phylogenetically closely affiliated to one of the cytosolic GAPDH and spermatogenic GAPDH-S of mammals. This indicates that the two paralogous GAPDH genes shared a common ancestor and subsequently underwent a gene duplication event during early vertebrate evolution. However, GAPDH-S of teleosts showed significant differences in the polypeptide residues and tissue distribution of its mRNA transcripts from that of mammals, implying they have undergone a different history of functionalization.
Abstract
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a key enzyme for carbohydrate meta-bolism in most living organisms. Recent reports and our own searches of teleost species in publicly available genomic databases have identified at least two distinct GAPDH genes in a given species. The two GAPDH genes are located on the same chromosome in teleosts, whereas they are located on the different chromosomes in mammals. Thus, we reconstructed a phy-logenetic tree to better understand the evolutionary history of the GAPDH genes in the vertebrate lineage. Our phylogenetic analysis revealed unambiguously that the two GAPDH genes of teleosts are phylogenetically closely affiliated to one of the cytosolic GAPDH and spermatogenic GAPDH-S of mammals. This indicates that the two paralogous GAPDH genes shared a common ancestor and subsequently underwent a gene duplication event during early vertebrate evolution. However, GAPDH-S of teleosts showed significant differences in the polypeptide residues and tissue distribution of its mRNA transcripts from that of mammals, implying they have undergone a different history of functionalization.
참고문헌 (18)
- Blomme, T., "The gain and loss of genes during 600 million years of vertebrate evolution", Genome Biology, 7, pp.B43~ (2006)
- Chuang, D.M, "Gly-ceraldehyde 3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases", Annual Review of Pharmacology and Toxicology, 45, pp.269~290 (2005)
- Felsenstein,J, "Confidence limits on phylogenies: an approach using the bootstrap", Evolution, 39, pp.783~791 (1985)
- Figge, R.M, "Glyceraldehyde 3-phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: evidence for intra- and inter-kingdom gene transfer", Molecular Biology and Evolution, 16, pp.429~440 (1999)
- Holland, J.P, "Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehy-drogenase gene families: the primary structure of a third yeast glyceraldehydes 3-phosphate dehydro-genase gene", The Journal of Biological Chemistry, 258, pp.5291~5299 (1983)
- Huang, X.-Y, "Genomic organization of the glyceraldehydes 3-phosphate de-hydrogenase gene family of Caenorhabditis elegans", Journal of Molecular Biology, 206, pp.411~424 (1989)
- Liaud, M.-F, "Compartment-specific isoforms of TPI and GAPDH are imported into diatom mitochondria as a fusion protein: evidence in favor of a mitochondrial origin of the eukaryotic glycolytic pathway", Molecular Biology and Evolution, 17, pp.213~223 (2000)
- Manchado, M, "Differential gene expression and dependence on thyroid hormones of two glyceraldehydes 3-phosphate dehydrogenases in the flatfish Senegalese sole (Solea senegalensis Kaup)", Gene, 400, pp.1~8 (2007)
- Martin, W, "Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehydes 3-phosphate dehydrogenase genes", Proceedings of the National Academy of Sciences of the United States of America, 90, pp.8692~8696 (1993)
- Miki, K, "Glyceraldehyde 3-phosphate dehydro-genase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility", Proceedings of the National Academy of Sciences of the United States of America, 101, pp.16501~16506 (2004)
- Petersen, J, "Origin, evolution, and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids", Journal of Molecular Evolution, 57, pp.16~26 (2003)
- Sirover,M.A, "New insights into an old protein: the functional diversity of mammalian glyceraldehydes 3-phosphate dehydrogenase", Biochimica et Biophysica Acta, 1432, pp.159~184 (1999)
- Sirover,M.A, "New nuclear functions of the gly-colytic protein, glyceraldehydes 3-phosphate dehydro-genase, in mammalian cells", Journal of Cellular Biochemistry, 95, pp.45~52 (2005)
- Steinke, D, "Three rounds (1R", 2R, BMC Biology, pp.2006, 4[DOI]
- Swofford,D.L, "PAUP: Phylogenetic Analysis Using Parsimony (and Other Methods). Ver 4.0b10" (2002), Sinauer Associates Inc
- Tso, J.Y, "Structure of two unlinked Drosophila melanogaster glyceraldehydes 3-phosphate dehydrogenase genes", The Journal of Biological Chemistry, 260, pp.8220~8228 (1985)
- Welch, J.E, "Expression of the spermatogenic cell-specific glyceraldehyde 3-phosphate dehydro-genase (GAPDS) in rat testis", Molecular Reproduction and Development, 73, pp.1052~1060 (2006)
- Xia, X, "DAMBE: Data analysis in molecular biology and evolution", Journal of Heredity, 92, pp.371~373 (2001)
