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Am J Physiol Renal Physiol 279: F866-F873, 2000;
0363-6127/00 $5.00
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Vol. 279, Issue 5, F866-F873, November 2000

Mapping and functional analysis of an instability element in phosphoenolpyruvate carboxykinase mRNA

Omar F. Laterza1, Lynn Taylor1, Shashikala Unnithan2, Ly Nguyen1, and Norman P. Curthoys1

1 Department of Biochemistry and Molecular Biology, Colorado State University, Ft. Collins 80523-1870; and 2 Department of Natural, Applied, and Environmental Sciences, Front Range Community College, Fort Collins, Colorado 80526

Phosphoenolpyruvate carboxykinase (PEPCK) is a key regulatory enzyme of renal gluconeogenesis. The 3'-nontranslated region of the PEPCK mRNA contains an instability element that facilitates its rapid turnover and contributes to the regulation of PEPCK gene expression. Such processes are mediated by specific protein-binding elements. Thus RNA gel shift analysis was used to identify proteins in rat renal cortical cytosolic extracts that bind to the 3'-nontranslated region of the PEPCK mRNA. Deletion constructs were then used to map the binding interactions to two adjacent RNA segments (PEPCK-6 and PEPCK-7). However, competition experiments established that only the binding to PEPCK-7 was specific. Functional studies were performed by cloning similar segments in a luciferase reporter construct, pLuc/Zeo. This analysis indicated that both PEPCK-6 and PEPCK-7 segments were necessary to produce a decrease in luciferase activity equivalent to that observed with the full-length 3'-nontranslated region. Thus the PEPCK-7 segment binds a specific protein that may recruit one or more proteins to form a complex that mediates the rapid decay of the PEPCK mRNA.

LLC-PFK1-F+ cells; ribonucleic acid-binding protein; messenger ribonucleic acid turnover


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