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J Biol Chem, Vol. 274, Issue 36, 25266-25272, September 3, 1999

Protein-RNA Interactions Determine the Stability of the Renal NaPi-2 Cotransporter mRNA and Its Translation in Hypophosphatemic Rats

From the Minerva Center for Calcium and Bone Metabolism, Nephrology Services, Hadasssah University Hospital, Jerusalem 91120, Israel

Hypophosphatemia leads to an increase in type II Na⁺-dependent inorganic phosphate cotransporter (NaPi-2) mRNA and protein levels in the kidney and increases renal phosphate reabsorption. Nuclear transcript run-on experiments showed that the effect of a low phosphate diet was post-transcriptional. In an in vitro degradation assay, renal proteins from hypophosphatemic rats stabilized the NaPi-2 transcript 6-fold compared with control rats and this was dependent upon an intact NaPi-2 3'-untranslated region (UTR). To determine an effect of hypophosphatemia upon NaPi-2 protein synthesis, the incorporation of injected [³⁵S]methionine into renal proteins was studied in vivo. Hypophosphatemia led to increased [³⁵S]methionine incorporation only into NaPi-2 protein. The effect of hypophosphatemia on translation was studied in an in vitro translation assay, where hypophosphatemic renal proteins led to increased translation of NaPi-2 and other transcripts. NaPi-2 RNA interaction with cytosolic proteins was studied by UV cross-linking and Northwestern gels. Hypophosphatemic proteins led to increased binding of renal cytosolic proteins to the 5'-UTR of NaPi-2 mRNA. Therefore, hypophosphatemia increases NaPi-2 gene expression post-transcriptionally, which correlates with a more stable transcript mediated by the 3'-UTR, and an increase in NaPi-2 translation involving protein binding to the 5'-UTR. These findings show that phosphate regulates gene expression by affecting protein-RNA interactions in vivo.

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