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Reconstruction of Cyclooxygenase Evolution in Animals Suggests Variable, Lineage-Specific Duplications, and Homologs with Low Sequence Identity
Department of Biology, Colorado State University.
School of Biological Sciences, The University of Queensland.
Auburn University, Department of Biological Sciences.
Swedish Museum of Natural History, Department of Zoology.
Show others and affiliations
2015 (English)In: Journal of Molecular Evolution, ISSN 0022-2844, E-ISSN 1432-1432, Vol. 80, p. 193-208Article in journal (Refereed) Published
Abstract [en]

Cyclooxygenase (COX) enzymatically converts arachidonic acid into prostaglandin G/H in animals and has importance during pregnancy, digestion, and other physio- logical functions in mammals. COX genes have mainly been described from vertebrates, where gene duplications are common, but few studies have examined COX in inverte- brates. Given the increasing ease in generating genomic data, as well as recent, although incomplete descriptions of potential COX sequences in Mollusca, Crustacea, and In- secta, assessing COX evolution across Metazoa is now possible. Here, we recover 40 putative COX orthologs by searching publicly available genomic resources as well as *250 novel invertebrate transcriptomic datasets. Results suggest the common ancestor of Cnidaria and Bilateria 

possessed a COX homolog similar to those of vertebrates, although such homologs were not found in poriferan and ctenophore genomes. COX was found in most crustaceans and the majority of molluscs examined, but only specific taxa/lineages within Cnidaria and Annelida. For example, all octocorallians appear to have COX, while no COX ho- mologs were found in hexacorallian datasets. Most species examined had a single homolog, although species-specific COX duplications were found in members of Annelida, Mollusca, and Cnidaria. Additionally, COX genes were not found in Hemichordata, Echinodermata, or Platyhelminthes, and the few previously described COX genes in Insecta lacked appreciable sequence homology (although structural analyses suggest these may still be functional COX en- zymes). This analysis provides a benchmark for identifying COX homologs in future genomic and transcriptomic data- sets, and identifies lineages for future studies of COX. 

Place, publisher, year, edition, pages
2015. Vol. 80, p. 193-208
National Category
Biological Sciences
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URN: urn:nbn:se:nrm:diva-1468DOI: DOI: 10.1007/s00239-015-9670-3OAI: oai:DiVA.org:nrm-1468DiVA, id: diva2:876109
Available from: 2015-12-02 Created: 2015-12-02 Last updated: 2017-12-01Bibliographically approved

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