J. Anim Sci.
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Published online first on July 3, 2008
J. Anim Sci. 1910. doi:10.2527/jas.2007-0798
© 2008 American Society of Animal Science
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Translational efficiency of bovine pyruvate carboxylase 5’ untranslated region mRNA variants

Sarah R. Hazelton, Stephanie L. Koser, Christopher A. Bidwell and Shawn S. Donkin

Department of Animal Sciences, 915 W. State Street, Purdue University, West Lafayette, IN 47907-2054

sdonkin{at}purdue.edu

Abstract

The bovine pyruvate carboxylase (PC) gene is expressed as six alternatively spliced variants that share a common open reading frame, but differ within their 5’ untranslated regions (UTR). The PC 5’ UTR variants (A through F) contain six combinations of five exons and are 68, 253, 363, 89, 226, 178 bp in length, respectively. The objective of this experiment was to determine if the bovine PC mRNA variants exhibit different translational efficiencies. Each bovine PC 5’UTR variant was linked to the firefly luciferase coding region, and the resulting constructs were transcribed and translated in a rabbit reticulocyte lysate assay. All constructs resulted in synthesis of luciferase protein. The abundance of luciferase protein synthesized from the UTR of bovine PC 5’D was greater (P < 0.05) than synthesis from either PC 5’ UTR C or E and the ability of UTR D, A, B, and F to drive protein translation were similar. The disproportionate contribution of the PC 5’ D UTR compared with UTR variant C or E to protein synthesis indicates a complexity of control for PC enzyme synthesis in bovine that is dependent on the profile of PC variants. These observations are consistent with differences in PC variant expression that have been observed in vivo and indicate that when PC mRNA is elevated the pattern of variants directs an increase in PC activity through augmented PC enzyme synthesis.

Key Words: bovine • liver • pyruvate carboxylase • translational efficiency • untranslated region,






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