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Research Paper
Regulation of Unr Expression by 5'- and 3'-Untranslated Regions of its mRNA through Modulation of Stability and IRES Mediated Translation
Virginie Dormoy-Raclet, Judith Markovits, Alain Jacquemin-Sablon and Helene Jacquemin-Sablon
volume 2 | issue 3
july/august/september 2005Pages: 112 - 120
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Unr (Upstream of N-Ras) is a cytoplasmic RNA-binding protein that can act as a regulator of mRNA stability and IRES-mediated translation. Unr, a member of the cold-shock domain (CSD) protein super-family, is ubiquitously expressed, with variable abundance, in different tissues or during embryonic development. Prokaryotic and eukaryotic cold-shock protein expression is highly regulated at both the transcriptional and post-transcriptional levels. Here we analyzed the role of the 5'- and 3'-untranslated regions (UTR) of unr mRNA in post-transcriptional regulation of Unr expression. We show that, in vitro, unr 3'-UTR specifically destabilizes unr transcripts. Accordingly, in vivo, the half-life of unr messages deleted of non-coding regions is increased by ~3.6 fold, resulting in an enhanced steady-state level of Unr protein. We also show that the 5'-UTR exhibits IRES activity both when translated in vitro and in transiently transfected cells. This IRES activity displays cell type specificity with a higher efficiency in HeLa and HuH7 than in ES cells. Moreover, Unr IRES activity was higher in unr-/- than in unr+/+ ES cells, indicating that Unr negatively regulates its own IRES activity. Our studies further reveal that Unr specifically interacts with its own mRNAs in vivo. These results suggest that a feedback control of mRNA translation is involved in regulating Unr expression.
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.