Identification of a novel dehydration responsive gene, drp10, from the African clawed frog, Xenopus laevis. Issue 6 (10th April 2015)

• Record Type: Journal Article
• Authors: Biggar, Kyle K.; Biggar, Yulia; Storey, Kenneth B.
• Is Part Of: Journal of experimental zoology. Volume 323:Issue 6(2015)
• Page Start: 375
• Page End: 381
• Publication Date: 2015-04-10
• Subjects: Zoology -- Periodicals; Ecological genetics -- Periodicals; Ecophysiology -- Periodicals; 571.105
• DOI: 10.1002/jez.1930
• Languages: English
• ISSNs: 1932-5223

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="jez1930-sec-0001" sec-type="section"> <p>During periods of environmental stress a number of different anuran species employ adaptive strategies to promote survival. Our study found that in response to dehydration (i.e., loss of total body water content), the African clawed frog (<italic>Xenopus laevis</italic>) increased the expression of a novel gene (<italic>drp10</italic>) that encodes a structural homolog of the freeze‐responsive FR10 protein found in wood frogs. Similar to FR10, the DRP10 protein was found to also contain a highly conserved N‐terminal cleavable signal peptide. Furthermore, DRP10 was found to have high structural homology to the available crystal structures of type A and E apolipoproteins in <italic>Homo sapiens</italic>, and a type IV LS‐12 anti‐freeze protein in the longhorn sculpin, <italic>Myoxocephalus octodecemspinosis</italic>. In response to dehydration, the transcript expression of <italic>drp10</italic> was found to increase 1.52 ± 0.16‐fold and 1.97 ± 0.11‐fold in response to medium (15%) and high (30%) dehydration stresses in the liver tissue of <italic>X. laevis</italic>, respectively, while <italic>drp10</italic> expression increased 2.12 ± 0.12‐fold and 1.46 ± 0.16‐fold in kidney tissue. Although the molecular function of both dehydration‐responsive DRP10 and the freeze‐responsive FR10 have just begun to be elucidated, it is likely that both are frog‐specific proteins that likely share a similar purpose during water‐related stresses. <italic>J. Exp. Zool. 323A: 375–381, 2015</italic>. © 2015 Wiley Periodicals, Inc.</p> </sec> </abstract>