Characterization of purine catabolic pathway genes in coelacanths. Issue 6 (3rd June 2013)

• Record Type: Journal Article
• Authors: Forconi, Mariko; Biscotti, Maria Assunta; Barucca, Marco; Buonocore, Francesco; De moro, Gianluca; Fausto, Anna Maria; Gerdol, Marco; Pallavicini, Alberto; Scapigliati, Giuseppe; Schartl, Manfred; Olmo, Ettore; Canapa, Adriana; Amemiya, Chris; Meyer, Axel
• Is Part Of: Journal of experimental zoology. Volume 322:Issue 6(2014)
• Page Start: 334
• Page End: 341
• Publication Date: 2013-06-03
• Subjects: Developmental biology -- Periodicals; Evolution (Biology) -- Periodicals; Molecular evolution -- Periodicals; Zoology -- Periodicals; Evolution, Molecular -- Periodicals; Developmental Biology -- Periodicals; Zoology -- Periodicals; 591
• DOI: 10.1002/jez.b.22515
• Languages: English
• ISSNs: 1552-5007

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="jezb22515-sec-0001" sec-type="section"> <p>Coelacanths are a critically valuable species to explore the gene changes that took place in the transition from aquatic to terrestrial life. One interesting and biologically relevant feature of the genus <italic>Latimeria</italic> is ureotelism. However not all urea is excreted from the body; in fact high concentrations are retained in plasma and seem to be involved in osmoregulation. The purine catabolic pathway, which leads to urea production in <italic>Latimeria</italic>, has progressively lost some steps, reflecting an enzyme loss during diversification of terrestrial species. We report the results of analyses of the liver and testis transcriptomes of the Indonesian coelacanth <italic>Latimeria menadoensis</italic> and of the genome of <italic>Latimeria chalumnae</italic>, which has recently been fully sequenced in the framework of the coelacanth genome project. We describe five genes, <italic>uricase</italic>, <italic>5‐hydroxyisourate hydrolase</italic>, <italic>parahox neighbor B</italic>, <italic>allantoinase</italic>, and <italic>allantoicase</italic>, each coding for one of the five enzymes involved in urate degradation to urea, and report the identification of a putative second form of <italic>5‐hydroxyisourate hydrolase</italic> that is characteristic of the genus <italic>Latimeria</italic>. The present data also highlight the activity of the complete purine pathway in the coelacanth liver and suggest its involvement in the maintenance of high plasma urea concentrations. <italic>J. Exp. Zool. (Mol. Dev. Evol.) 322B: 334–341, 2014</italic>. © 2013 Wiley Periodicals, Inc.</p> </sec> </abstract>