Phylogenetic analysis of glycerol 3-phosphate acyltransferases in opisthokonts reveals unexpected ancestral complexity and novel modern biosynthetic components

Glycerolipid synthesis represents a central metabolic process of all forms of life. In the last decade multiple genes coding for enzymes responsible for the first step of the pathway, catalyzed by glycerol 3-phosphate acyltransferase (GPAT), have been described, and characterized primarily in model...

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Bibliographic Details
Published in:PloS one 2014-10, Vol.9 (10), p.e110684
Main Authors: Smart, Heather C, Mast, Fred D, Chilije, Maxwell F J, Tavassoli, Marjan, Dacks, Joel B, Zaremberg, Vanina
Format: Article
Language:English
Subjects:
Acyltransferase
Amino Acid Motifs
Amino Acid Sequence
Analysis
Animals
Baking yeast
Biocatalysis
Biology and Life Sciences
Biosynthesis
Cells (Biology)
Cladistic analysis
Complexity
Divergence
Endoplasmic reticulum
Endoplasmic Reticulum - enzymology
Enzymes
Eukaryota - enzymology
Evolution
Fungi
Fungi - enzymology
Gene Duplication
Genomes
Genomics
Glycerol
Glycerol-3-Phosphate O-Acyltransferase - chemistry
Glycerol-3-Phosphate O-Acyltransferase - metabolism
Glycolipids - biosynthesis
Homeostasis
Homology
Humans
Intracellular Space - metabolism
Isoenzymes - metabolism
Isoforms
Lipid metabolism
Lipids
Mammals
Metabolism
Metabolites
Mitochondria
Mitochondria - enzymology
Models, Biological
Molecular Sequence Data
Organisms
Phosphates
Phylogenetics
Phylogeny
Proteins
Saccharomyces cerevisiae
Sequence Homology, Amino Acid
Species Specificity
Synthetic biology
Transferases
Yeast
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Summary:Glycerolipid synthesis represents a central metabolic process of all forms of life. In the last decade multiple genes coding for enzymes responsible for the first step of the pathway, catalyzed by glycerol 3-phosphate acyltransferase (GPAT), have been described, and characterized primarily in model organisms like Saccharomyces cerevisiae and mice. Notoriously, the fungal enzymes share low sequence identity with their known animal counterparts, and the nature of their homology is unclear. Furthermore, two mitochondrial GPAT isoforms have been described in animal cells, while no such enzymes have been identified in Fungi. In order to determine if the yeast and mammalian GPATs are representative of the set of enzymes present in their respective groups, and to test the hypothesis that metazoan orthologues are indeed absent from the fungal clade, a comparative genomic and phylogenetic analysis was performed including organisms spanning the breadth of the Opisthokonta supergroup. Surprisingly, our study unveiled the presence of 'fungal' orthologs in the basal taxa of the holozoa and 'animal' orthologues in the basal holomycetes. This includes a novel clade of fungal homologues, with putative peroxisomal targeting signals, of the mitochondrial/peroxisomal acyltransferases in Metazoa, thus potentially representing an undescribed metabolic capacity in the Fungi. The overall distribution of GPAT homologues is suggestive of high relative complexity in the ancestors of the opisthokont clade, followed by loss and sculpting of the complement in the descendent lineages. Divergence from a general versatile metabolic model, present in ancestrally deduced GPAT complements, points to distinctive contributions of each GPAT isoform to lipid metabolism and homeostasis in contemporary organisms like humans and their fungal pathogens.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0110684