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Am J Physiol Renal Physiol 278: F970-F977, 2000;
0363-6127/00 $5.00
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Vol. 278, Issue 6, F970-F977, June 2000

Specificity and functional analysis of the pH-responsive element within renal glutaminase mRNA

Omar F. Laterza and Norman P. Curthoys

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870

The specificity and the functional significance of the binding of a specific cytosolic protein to a direct repeat of an eight-base AU sequence within the 3'-nontranslated region of the glutaminase (GA) mRNA were characterized. Competition experiments established that the protein that binds to this sequence is not an AUUUA binding protein. When expressed in LLC-PK1-F+ cells, the half-life of a beta -globin reporter construct, beta G-phosphoenolpyruvate carboxykinase, was only slightly affected (1.3-fold) by growth in acidic (pH 6.9, 10 mM HCO-3) vs. normal (pH 7.4, 25 mM HCO-3) medium. However, insertion of short segments of GA mRNA containing the direct repeat or a single eight-base AU sequence was sufficient to impart a fivefold pH-responsive stabilization to the chimeric mRNA. Furthermore, site-directed mutation of the direct repeat of the 8-base AU sequence in a beta G-GA mRNA, which contains 956 bases of the 3'-nontranslated region of the GA mRNA, completely abolished the pH-responsive stabilization of the wild-type beta G-GA mRNA. Thus either the direct repeat or a single eight-base AU sequence is both sufficient and necessary to create a functional pH-response element.

LLC-PK1-F+ cells; proximal tubule; metabolic acidosis; renal ammoniagenesis


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